MOLECULAR BIOLOGY OF THE CELL, SIXTH EDITION

CHAPTER 16: THE CYTOSKELETON

© Garland Science 2015

1. Indicate if each of the following structures is based on actin filaments (A), microtubules
(M), or intermediate filaments (I). Your answer would be a five-letter string composed of letters
A, M, and I only; e.g. AAAMM.
( ) The cell cortex
( ) The mitotic spindle
( ) The nuclear lamina
( ) Cilia
( ) Filopodia

2. Indicate if each of the following changes occurring during mitosis in a fibroblast is the
result of the reorganization of actin filaments (A), microtubules (M), or intermediate filaments
(I). Your answer would be a five-letter string composed of letters A, M, and I only; e.g. AIAAM.
( ) The cell rounds up.
( ) The endoplasmic reticulum collapses.
( ) The Golgi apparatus fragments.
( ) The primary cilium is resorbed (disappears).
( ) The contractile ring forms and constricts.

3. Which of the following cytoskeletal filaments are abundant in an animal cell nucleus?
A. Microfilaments
B. Microtubules
C. Septins
D. Intermediate filaments
E. Spectrin filaments

4. From left to right, indicate if each of the following schematic drawings represents the
typical overall organization of actin filaments (A), microtubules (M), or intermediate filaments
(I) in an animal cell. Your answer would be a three-letter string composed of letters A, M, and I
only; e.g. AMI.
5. Indicate true (T) and false (F) statements below regarding the cell cytoskeleton. Your
answer would be a four-letter string composed of letters T and F only; e.g. TTFF.
( ) The three major building blocks of cytoskeletal filaments can bind to and hydrolyze
nucleotides.
( ) The building blocks of microfilaments and microtubules are globular proteins,
whereas those of intermediate filaments are themselves filamentous proteins.
( ) Intermediate filaments are typically thicker than actin filaments but thinner than
microtubules.
( ) Plant cells lack microtubules.

6. Fill in the blank: Each microtubule is typically made of thirteen parallel …. that associate
laterally to form a hollow tube.

7. Indicate if each of the following descriptions matches actin filaments (A), microtubules
(M), or intermediate filaments (I). Your answer would be a four-letter string composed of letters
A, M, and I only; e.g. AAMM.
( ) They form hollow structures with multiple lateral interactions.
( ) They form strong structures that are more resilient than the other two cytoskeletal
filaments.
( ) Their subunits bind GTP and hydrolyze it.
( ) They form coiled-coil interactions between the subunits.

8. Bacteria contain homologs of cytoskeletal filament subunits …

 A. except those of the intermediate filaments.
B. but these homologs are incapable of nucleotide binding and hydrolysis.
C. that are less diverse in their function relative to their eukaryotic counterparts.
D. that can have different functions to those of their eukaryotic counterparts.
E. that are dispensable for cell growth and proliferation.

9. Persistence length for a cytoskeletal filament is the minimum filament length at which
random thermal fluctuations are likely to cause it to bend. Which of the following comparisons
are true, considering the persistence lengths of (a) an actin filament, (b) a bundle of cross-linked
actin filaments, and (c) a microtubule?
A. (a > b) and (a > c)
B. (a > b) and (a < c)
C. (a < b) and (a > c)
D. (a < b) and (a < c)
E. (a > b) and (b > c)

10. You have prepared actin filament seeds in a microfluidic chamber through which you
then pass either unlabeled or fluorescently labeled actin subunits in alternation several times,
keeping the total monomer concentration constant. You then observe the resulting filaments
under a fluorescence microscope. If the filaments appear as drawn schematically in the example
below (in which fluorescence is indicated by black color), which end do you think is the plus
end—(a) or (b)? Was the concentration of free actin subunits below or above the critical
concentration (Cc) for polymerization at the barbed end?

(b)

(a)

A. (a); below
B. (b); below
C. (a); above
D. (b); above
11. F-actin is not a straight polymer but can be considered a double-helical assembly. The
two protofilaments twist around each other and cross over approximately every 13 actin subunits,
and the subunits in each protofilament are repeated every 2.8 nm along the helix. F-actin is
almost 8 nm wide. Different myosin motors have different “step lengths” on actin depending on
their function. Which of the following step lengths would you expect to belong to a processive
myosin motor that carries large cellular cargoes such as endocytic vesicles?
A. About 2.8 nm
B. About 8 nm
C. About 13 nm
D. About 27 nm
E. About 36 nm

12. In the polymerization in vitro of actin filaments and microtubules from their subunits,
what does the “lag phase” correspond to?
A. Nucleation
B. Reaching steady state
C. Nucleotide exchange
D. ATP or GTP hydrolysis
E. Treadmilling

13. The time courses of seeded actin polymerization under two different conditions are
compared in the following graph. If the overall kon for polymerization is known to be the same
under both of these conditions, which curve—(1) or (2)—corresponds to the condition with a
higher koff rate constant? Which one corresponds to a higher Cc for polymerization?

(1)
subunits in filaments
Percentage of actin

(2)

Time after salt addition

 A. Curve (1); curve (1)
B. Curve (1); curve (2)
C. Curve (2); curve (1)
D. Curve (2); curve (2)
E. Curve (2); both curves have the same Cc.

14. If the concentration of free subunits is C, under which condition does the growth of a
cytoskeletal filament proceed spontaneously?
A. C > 1/kon
B. C < 1/koff
C. C > kon/koff
D. C > koff/kon
E. C > Cc×kon/koff

15. Consider the ATP-bound and ADP-bound forms of actin and the polarized nature of the
actin filaments. In the following diagram that shows the various actin polymerization rate
constants (kon and koff values), which monomer corresponds to an ADP-bound actin incorporated
at the plus end?

(A) (C)
–1 –1 –1 –1
0.1 µM sec 12 µM sec

0.3 sec–1 1.5 sec–1

1.5 µM–1.sec–1 4 µM–1 sec–1

0.8 sec–1 8 sec–1
(B) (D)

16. In the following graph of actin elongation rates under different subunit concentrations,
which of the following corresponds to the slope of the line?
 grow

Elongation rate 0

shrink
Subunit concentration

A. kon
B. koff
C. kon/koff
D. koff/kon
E. kon – koff

17. According to the following graph, which shows the elongation rate at the plus and minus
ends of actin filaments as a function of actin subunit concentration, at what concentration (A to
E) does the total length of the filament remain more or less constant with time (i.e. steady-state
treadmilling occurs)?

grow
Elongation rate

shrink
A B C D E
Subunit concentration
18. Which of the following drugs is toxic for our cells?
A. Cytochalasin B, which caps the plus end of actin filaments and prevents actin
polymerization.
B. Phalloidin, which binds along actin filaments and stabilizes them.
C. Nocodazole, which binds to tubulin subunits and prevents microtubule
polymerization.
D. Colchicine, which caps microtubule ends and leads to their depolymerization.
E. All of the above.

19. The actin-nucleating protein formin has flexible “whiskers” containing binding sites that
help recruit actin subunits in order to enhance polymerization by this protein. What protein
would you expect to bind to these sites?
A. Thymosin
B. Profilin
C. Cofilin
D. Gelsolin
E. Tropomodulin

20. Which of the following is an actin homolog?

A. Arp2
B. Arp3
C. MreB
D. ParM
E. All of the above

21. Which of the following actin-binding proteins cannot bind to the same actin filament
simultaneously?
A. Gelsolin and tropomodulin
B. Tropomyosin and tropomodulin
C. Profilin and tropomodulin
D. Cofilin and CapZ
E. Formin and CapZ

22. In the following graph, the elongation rate of pure actin filaments as a function of actin
subunit concentration is shown as a dashed line. Which one of the other five lines (A to E) would
you think better shows what happens when a plus-end capping protein such as CapZ is present?
 grow
A

Elongation rate
B
C
D
0

shrink E

Subunit concentration

23. Which of the actin-binding proteins (1 to 5) in the following schematic drawing

represents tropomyosin, α-actinin, Arp 2/3 complex, CapZ, and myosin, respectively? Your
answer would be a five-digit number composed of digits 1 to 5 only; e.g. 15324.

(1)
(+) end (–) end

(3) (4) (2)

(5)

(–) end (+) end

24. Cofilin binds preferentially to ADP-containing actin filaments rather than to ATP-
containing filaments. Consequently, this protein …
A. competes with profilin for actin binding.
B. binds to older actin filaments.
C. binds to the plus end of actin filaments.
D. stabilizes actin filaments.
E. All of the above.
25. Actin filaments that are held together by the cross-linking protein fimbrin are not
contractile. This is probably because …
A. the very weak cross-linking by this protein cannot convert myosin II activity into a
coherent contraction.
B. fimbrin arranges the actin filaments in parallel bundles in which all the plus ends
point to the same direction.
C. the very tight packing of actin filaments by this small protein excludes myosin II
filaments and other large proteins.
D. fimbrin arranges the actin filaments into gel-like networks in which myosin II activity
does not produce contraction.
E. fimbrin is a large protein that binds to several actin filaments and resists contraction.

26. In the dendritic networks of actin filaments in lamellipodia, nucleation of actin

polymerization is mostly performed by …
A. ERM proteins
B. WASp proteins
C. Formin
D. Arp 2/3 complex
E. γ-TuRC

27. In the structure of which of the following proteins are the actin-filament binding sites
furthest apart in space?
A. Spectrin
B. Filamin
C. α-Actinin
D. Fimbrin
E. Myosin II

28. The proteins of the ERM family such as moesin …

A. bind to and organize the cortical actin cytoskeleton.
B. interact with transmembrane proteins.
C. affect cortical stiffness and cell shape.
D. affect the localization and activity of cell signaling molecules.
E. All of the above.
29. The pathogen Listeria monocytogenes can hijack the actin cytoskeleton in human cells
and spread inside the host. Indicate true (T) and false (F) statements below about this
phenomenon. Your answer would be a four-letter string composed of letters T and F only; e.g.
TTFF.
( ) The movement can be reconstituted in vitro by placing the bacteria in a mixture of
actin, formin, gelsolin, and capping protein.
( ) Cofilin counteracts the movement by depolymerizing actin filaments.
( ) The actin filaments grow with their minus ends pointed toward the bacterium.
( ) The movement depends on myosin activity to transport the bacteria on the actin
filaments.

30. Indicate true (T) and false (F) statements below regarding cytoskeletal motor proteins.
Your answer would be a five-letter string composed of letters T and F only, e.g. TTTFF.
( ) All myosin motors move toward the plus end of actin filaments.
( ) All myosin motors move toward the minus end of actin filaments.
( ) All kinesin motors move toward the plus end of microtubules.
( ) All kinesin motors move toward the minus end of microtubules.
( ) All dynein motors move toward the minus end of microtubules.

31. If myosin II heads are attached to a glass slide and actin filaments are allowed to bind to
them, the filaments will glide on the surface …
A. toward their plus end in the presence of ATP.
B. toward their plus end in the presence of GTP.
C. toward their minus end in the presence of ATP.
D. toward their minus end in the presence of GTP.
E. toward their plus end in the presence of ADP.

32. Sort the following events to show the sequence in the mechanochemical cycle of myosin
II, following ATP binding by the head domain. Your answer would be a four-digit number
composed of digits 1 to 4 only, e.g. 1342.
(A) Myosin head binds tightly to actin.
(B) Power stroke is triggered.
(C) Cocking occurs and the head is displaced along the actin filament.
(D) The binding affinity of myosin for actin is reduced.
33. In the presence of an ATP analog that can bind myosin normally but cannot be
hydrolyzed, …
A. a myosin cannot bind tightly to an actin filament and cannot move on it.
B. a myosin cannot be released from an actin filament and cannot move on it.
C. a myosin performs the power stroke but cannot be released from an actin filament.
D. a myosin performs the power stroke but cannot bind tightly to an actin filament.
E. a myosin is able to perform normally.

34. After an animal dies, its muscles start to stiffen before the decomposition of tissues
relaxes the muscles again. Which of the following would you expect to explain this muscle
stiffening (i.e. rigor mortis)?
A. The myosin II heads in muscle fibers remain attached to actin filaments due to the
absence of Ca2+ in these cells.
B. The ATPase activity of muscle myosin II is inhibited by the elevated Ca2+.
C. The myosin II heads in muscle cells remain attached to actin filaments due to the
elevated Ca2+ in the muscle fibers.
D. Titin molecules unfold, preventing muscle relaxation.
E. The myosin II heads in muscle cells remain attached to actin filaments due to
covalent cross-linking.

35. You have used “optical tweezers” to study the mechanics of myosin movement in a
newly discovered member of the myosin II subfamily. Your results indicate that each myosin
exerts a force of about 3 pN along the length of the actin filament, and displaces the filament by
about 10 nm in each cycle of ATP hydrolysis. Assuming that the free-energy change for ATP
hydrolysis is –50 kJ/mol under your experimental conditions, what is the efficiency of the
myosin motor in converting the free energy to mechanical work? Remember that under a
constant force F (in newtons), work (W; in joules) is calculated as W = F × d, where d is
displacement (in meters) in the direction of the force. Avogadro’s number is approximately 6 ×
1023 molecules/mole. Write down your answer as a percentage with no decimals, e.g. 99%.

36. Consider the structure of a sarcomere. Which of its features does NOT shorten during
skeletal muscle contraction?
A. The dark band
B. The light band
C. The distance from the M line to the Z disc
D. The distance between two consecutive Z discs
 E. The extension of the titin molecules

37. Skeletal muscle cells consume enormous amounts of ATP. From the following list,
choose the two proteins that directly hydrolyze most of this ATP. Your answer would be a two-
letter string composed of letters A to F only, in alphabetical order, e.g. AF.
A. Troponin complex
B. Ca2+-release channel
C. Myosin light chains
D. Myosin heavy chain
E. Myosin light-chain kinase
F. Sarcoplasmic reticulum Ca2+-pump

38. Heart conditions known as cardiomyopathies include two main subtypes, namely the
hypertrophic and dilated cardiomyopathies, in which some portions of the cardiac muscle
become stiff or dilated, respectively. Drugs such as the calcium channel blocker verapamil are
used to treat the former, while the Na+-K+ ATPase inhibitor digoxin (which elevates intracellular
calcium concentration in cardiac muscle cells) is sometimes used for the latter. Mutations in the
subunits of the troponin complex are among the genetic causes of these diseases, and can be
grouped into mutations that result in either decreased (D) or increased (I) calcium-ion sensitivity
of actin–myosin contraction. Which of these mutations would you expect to be associated with
hypertrophic cardiomyopathy? Write down D or I as your answer.

39. Sort the following events to reflect the sequence during smooth muscle contraction upon
delivery of muscle stimulation. Your answer would be a five-digit number composed of digits 1
to 5 only, e.g. 13452.
(A) Activation of the myosin light-chain kinase
(B) Interaction of myosin head with actin
(C) Phosphorylation of myosin
(D) Calcium release into the cytoplasm
(E) Activation of calmodulin

40. In which of the following structures are actin–myosin II bundles regulated by the
troponin complex?

A. Stress fiber
B. Circumferential belt
 C. Contractile ring
D. Adherens junction
E. None of the above

41. A small unique insert found near the end of the motor domain in myosin VI has been
linked to the singular ability of this myosin to move toward the pointed end of actin filaments. If
the unique insert is removed by genetic engineering, the resulting mutant myosin VI is a plus-end
directed motor. This observation indicates that …
A. the unique insert is necessary and sufficient for minus-end directionality.
B. the unique insert is necessary for motor activity.
C. the unique insert is necessary for plus-end directed directionality.
D. the unique insert is not sufficient for minus-end directionality.
E. None of the above.

42. The duty ratio for a motor protein is defined as the fraction of time in each cycle of
activity of the motor in which the head is bound with high affinity to its cytoskeletal track.
Which of the following is reasonable given this definition?
A. Myosin V has a higher duty ratio than myosin II, because Pi release is the rate-
limiting step in its cycle.
B. Myosin II has a higher duty ratio than myosin V, because Pi release is the rate-
limiting step in its cycle.
C. Myosin V has a higher duty ratio than myosin II, because ADP release is the rate-
limiting step in its cycle.
D. Myosin II has a higher duty ratio than myosin V, because ADP release is the rate-
limiting step in its cycle.

43. A microtubule appears as a left-handed helix due to an approximately 0.9-nm stagger in

the lateral contacts between adjacent protofilaments. In the lateral contacts, α- and β-tubulins in
one protofilament interact with α- and β-tubulins, respectively, in the neighboring protofilament,
except for a longitudinal discontinuity along the microtubule called the seam. Along the seam,
lateral contacts have to be made between different tubulins (i.e. α-tubulin with β-tubulin). Which
of the following do you think is acceptable as the repeat distance of tubulin monomers along a
protofilament?
A. 4 nm
B. 5 nm
 C. 6 nm
D. 7 nm
E. 10 nm

44. In the following graph that shows changes in the lengths of two microtubules over time,
which time point corresponds to a catastrophe for both microtubules? Which trace corresponds to
a microtubule with greater dynamic instability?

long
Microtubule length

(a)

(b)
short
0 t1 t2
Time

A. t1; trace (a)

B. t1; trace (b)
C. t2; trace (a)
D. t2; trace (b)

45. In contrast to growing microtubules, shrinking microtubules …

A. have a GTP cap at their plus end.
B. have strong lateral interactions at their plus ends.
C. have curved protofilaments at their plus ends.
D. cannot be rescued unless microtubule-stabilizing proteins bind and inhibit
depolymerization.
E. All of the above.

46. The γ-tubulin ring complex is to microtubules what … is to actin filaments.

 A. the Arp 2/3 complex
B. the dynactin complex
C. the troponin complex
D. formin
E. contractile ring

47. What is the major microtubule-organizing center in animal cells?

A. The γ-tubulin ring complex
B. The centrosome
C. The cell cortex
D. The primary cilium
E. The spindle pole body

48. Which of the following proteins do you expect to be enriched near the plus end of
microtubules?
A. Dynein
B. XMAP215
C. γ-Tubulin
D. Katanin
E. All of the above

49. Indicate if each of the following descriptions applies to (1) EB1, (2) kinesin-1, (3)
kinesin-13, or (4) katanin. Your answer would be a four-digit number composed of digits 1 to 4
only, e.g. 1432.
( ) This is a microtubule-severing protein that can release microtubules from the
microtubule-organizing centers.
( ) It increases the frequency of catastrophe by deforming microtubule protofilaments.
( ) This is a conventional motor protein that moves toward the plus end of a microtubule.
( ) It recognizes the structure of a growing microtubule end and binds to it, helping other
proteins to also bind to the plus end.

50. Indicate whether each of the following descriptions applies to myosins (M), kinesins (K),
or dyneins (D). Your answer would be a five-letter string composed of letters M, K, and D only,
e.g. MMMDD.
( ) They have larger structures than the other two.
( ) They are generally faster than the other two.
 ( ) They are structurally unrelated to the other two.
( ) They walk on a different cytoskeletal filament than the other two.
( ) They are all minus-end directed.

51. Unlike a myosin head, a kinesin head is tightly bound to its cytoskeletal track when
bound to ...
A. ATP.
B. ADP.
C. no nucleotide.
D. GTP.
E. GDP.

52. A dimeric kinesin-1 molecule has 8-nm steps and can move at rates of about 1 µm/sec.
Olympic 100-meter sprinters typically run at about 180 steps per minute and can reach speeds of
about 42 km/h. With the same step size, if the Olympic runner had a step frequency of a kinesin-
1 molecule, how fast could she run? Write down your answer in km/h, e.g. 52 km/h.

53. Dynamitin is a subunit of the dynactin complex. Its overexpression leads to the
disassembly of the complex, and it is therefore considered a dynactin inhibitor. Which of the
following processes would happen if dynamitin is overexpressed in a cell?
A. The motile cilia (if any) would stop beating because the axonemal dyneins could not
attach to their neighboring microtubules.
B. The Golgi apparatus would fragment and become dispersed because the cytoplasmic
dyneins could not associate with the Golgi membranes.
C. The endoplasmic reticulum would collapse because it could not recruit enough
kinesins.
D. The nuclear envelope would disintegrate because the nuclear lamins could not
interact with the cytoplasmic cytoskeleton.
E. The cortex would lose its integrity because the Arp 2/3 complex would also be
inhibited.

54. Using time-lapse fluorescence microscopy, you have recorded the transport of
fluorescently labeled mitochondria in a region of an axon in a fruit-fly larva; you have plotted the
results in the following graph, in which the vertical axis is time (from the top to the bottom), the
horizontal axis is the position along the axon, and each trace represents one mitochondrion. Is the
retrograde transport or the anterograde transport of mitochondria faster in these axons? Does the
trace indicated by an asterisk correspond to a mitochondrion that was transported by a dynein or
a kinesin?

Time *

toward the cell Position toward the tip

body of the axon

A. Anterograde; kinesin
B. Anterograde; dynein
C. Retrograde; kinesin
D. Retrograde; dynein

55. “Headless” kinesin mutants only contain the stalk (middle) and tail domains and can
therefore dimerize with their wild-type kinesin partners. However, since they lack the motor
(head) domain, the resulting dimers are unable to carry out processive transport of their cargoes
and the mutation thus behaves as “dominant negative,” meaning that the mutant not only is
nonfunctional, but can also interfere with the function of its wild-type counterparts. If a headless
mutant of a kinesin heavy chain involved in melanosome movement is overexpressed in fish
melanocytes, what would you predict happens in these cells?
A. Pigment dispersion would be inhibited and there would be more tug-of-war between
the motors.
B. Pigment aggregation would be inhibited and there would be more tug-of-war between
the motors.
C. Pigment dispersion would be inhibited and there would be less tug-of-war between
the motors.
D. Pigment aggregation would be inhibited and there would be less tug-of-war between
the motors.
56. Indicate true (T) and false (F) statements below regarding the microtubule cytoskeleton in
neurons. Your answer would be a five-letter string composed of letters T and F only, e.g. TTFFF.
( ) All microtubules in an axon are normally oriented in the same direction.
( ) All microtubules in a dendrite are normally oriented in the same direction.
( ) Each microtubule in an axon has one end at the cell body and its other end at the axon
terminal.
( ) Anterograde transport in axons is exclusively carried out by kinesins.
( ) Anterograde transport (toward the tip) in dendrites is exclusively carried out by
kinesins.

57. Indicate whether each of the following descriptions applies to cilia (C), flagella (F), or
both (B). Your answer would be a four-letter string composed of letters C, F, and B only, e.g.
CCFB.
( ) They are short and present at high numbers per cell.
( ) They have a whiplike motion that resembles breaststroke in swimming.
( ) They are based on the axoneme structure.
( ) They are found in the epithelial cells of the human respiratory tract.

58. In the presence of ATP in a flagellum, an axonemal dynein that is interacting through its
tail with the A microtubule of a peripheral doublet can push this doublet toward the ...(1) of the
flagellum, but due to the presence of linking proteins such as ...(2), this force is converted into a
bending motion.
A. (1) tip; (2) nexin
B. (1) base; (2) nexin
C. (1) tip; (2) nebulin
D. (1) base; (2) nebulin
E. (1) tip; (2) tau

59. Indicate true (T) and false (F) statements below regarding the primary cilia. Your answer
would be a four-letter string composed of letters T and F only, e.g. TFFF.
( ) Primary cilia are found on the surface of almost all cell types in our bodies.
( ) Primary cilia are motile.
( ) Primary cilia are made in interphase at basal bodies.
( ) Primary cilia are thought to function in sensing and responding to external signals.
60. Indicate whether each of the following descriptions matches actin filaments (A),
microtubules (M), or intermediate filaments (I). Your answer would be a three-letter string
composed of letters A, M, and I only, e.g. MMA.
( ) They have the smallest persistence length.
( ) They lack polarity.
( ) They have the highest tensile strength.

61. Keratins are intermediate filaments that ...

A. are localized inside the nucleus.
B. are composed of 50% type I and 50% type II keratin proteins.
C. are bundled in the epidermis to make cells more flexible.
D. anchor the intermediate filament network at the adherens junctions.
E. All of the above.

62. What are the typical consequences of mutations in keratins and their associated proteins?
A. Neurodegeneration as a result of interference with normal axonal transport.
B. Muscle development defects as a result of sarcomere disorganization.
C. Skeletal and cardiac abnormalities as a result of a weakened nuclear envelope.
D. Cornea disorders as a result of cell rupture from mechanical trauma.
E. Developmental defects as a result of abnormal signaling related to the primary cilia.

63. In a cross section of a vertebrate axon, longitudinally organized cytoskeletal proteins can
be seen as dots, as shown in the schematic drawing below. What type of filaments do these dots
represent?

A. Microtubules and microfilaments

B. Microtubules and vimentins
C. Microtubules and neurofilaments
D. Microtubules and keratins
 E. Microtubules and septins

64. These proteins are found in the budding yeast Saccharomyces cerevisiae; they form
“neck filaments” between a mother cell and its growing bud, and help polarize protein
distribution between the two. These proteins ...
A. can polymerize to form filaments and sheets.
B. bind GTP.
C. are also involved in contractile ring formation during cytokinesis in animal cells.
D. form filaments that are thought to be nonpolar.
E. All of the above.

65. SUN and KASH proteins embedded in the nuclear envelope provide connections between
the organization of the nucleus and the cytoplasm. Which of the following pairs of proteins DO
NOT bind directly to each other in these connections?
A. Nuclear lamina and SUN proteins
B. Plectins and KASH proteins
C. KASH proteins and microfilaments
D. KASH proteins and SUN proteins
E. SUN proteins and cytoplasmic intermediate filaments.

66. Which of the following is NOT an example of a crawling cell?

A. Macrophage
B. Osteoclast
C. Keratocyte
D. Neural crest cell
E. Sperm

67. Indicate whether each of the following structures has actin organized mostly in a one- (1),
two- (2), or three- (3) dimensional arrangement. Your answer would be a four-digit number
composed of digits 1 to 3 only, e.g. 1333.
( ) Stress fibers
( ) Invadopodia
( ) Lamellipodia
( ) Filopodia

68. How is membrane protrusion by blebbing different from that by lamellipodia?

 A. Blebbing usually occurs on a rigid substratum such as glass, whereas lamellipodia
form on pliable substrata.
B. Blebbing is mostly observed in vitro, whereas lamellipodia are observed both in vitro
and in vivo.
C. Blebbing does not involve myosin II activity, but formation of lamellipodia does.
D. Blebbing requires loss of membrane interaction with actin filaments, whereas
lamellipodia require a close interaction between the two.
E. All of the above.

69. Consider an actin subunit that has just been incorporated into an actin filament at the
leading edge of a lamellipodium. Before its ATP is hydrolyzed, how does its distance from the
leading front edge of the plasma membrane change over time? How does its distance from the F-
actin minus end change over time?
A. Decreases; decreases
B. Decreases; remains constant
C. Decreases; increases
D. Increases; decreases
E. Increases; remains constant

70. In the following schematic drawing, in which direction (1 or 2) is the keratocyte

migrating? What is the approximate length of the cell indicated by the bar on the left?

2
 A. Direction 1; about 20 µm
B. Direction 1; about 2 µm
C. Direction 2; about 20 µm
D. Direction 2; about 2 µm
E. Either direction; about 2 µm

71. If a certain isoform of myosin II is depleted from a cell, stress fibers are lost and focal
adhesions disappear. If these cells are placed on a surface coated with an array of flexible pillars
to measure traction forces, would you expect the traction to increase (I) or decrease (D) in these
cells compared to wild-type cells? Write down I or D as your answer.

72. In lamellipodia, actin polymerization is nucleated by ...(1), while depolymerization is

catalyzed by ...(2).
A. (1) formin; (2) gelsolin
B. (1) Arp 2/3 complex; (2) gelsolin
C. (1) formin; (2) cofilin
D. (1) Arp 2/3 complex; (2) cofilin
E. (1) formin; (2) capping protein

73. Indicate whether each of the following descriptions matches Cdc42 (C), Rac (R), or Rho
(H) from the Rho family of monomeric GTPases. Your answer would be a three-letter string
composed of letters C, R, and H only, e.g. HRR.
( ) It activates formin.
( ) It inhibits myosin II activity.
( ) When constitutively active, it induces the formation of many prominent stress fibers.

74. In the following schematic drawing of a polarized neutrophil engaged in chemotaxis, in

what region (a or b) does Rac activity dominate? What other member of the Rho family
dominates at the other region?
 Bacterial
peptides

a
b

A. Region (a); Rho

B. Region (a); Cdc42
C. Region (b); Rho
D. Region (b); Cdc42

75. Considering the diagram below, which summarizes two signaling pathways initiated by
activated GTPases of the Rho family, what letter (A to D) corresponds to each of the following?
Your answer would be a four-letter string composed of letters A to D only, e.g. ABCD.

A B

C
( ) Rac-GTP
( ) Rho-GTP
( ) Lamellipodia formation
( ) Stress-fiber formation
 Answers
1. Answer: AMIMA
Difficulty: 1
Section: Function and Origin of the Cytoskeleton
Feedback: Microtubules form cilia and flagella and are also responsible for the formation
of the bipolar mitotic spindle. Actin filaments underlie the plasma membrane of animal
cells and form dynamic structures such as filopodia. The nuclear lamina is an example of
structures formed by intermediate filaments to provide the cell interior with mechanical
strength.
2. Answer: AMMMA
Difficulty: 2
Section: Function and Origin of the Cytoskeleton
Feedback: The change in the organization of the actin-based cell cortex leads to round
cells that are later cleaved into two daughter cells by the actin-based contractile ring. The
network of endoplasmic reticulum membranes and Golgi stacks lose their interphase
distribution during mitosis as a result of a profound reorganization of the microtubules,
which also affects the microtubule-based primary cilia.
3. Answer: D
Difficulty: 1
Section: Function and Origin of the Cytoskeleton
Feedback: The lamins (one type of intermediate filament) form a meshwork beneath the
nuclear envelope called the nuclear lamina.
4. Answer: MIA
Difficulty: 2
Section: Function and Origin of the Cytoskeleton
Feedback: While the microtubule network usually has an overall radial distribution
during interphase, with the majority of the microtubules originating from the cell center,
the actin cytoskeleton forms the cell cortex near the cell periphery and is also found in
other places in the cell, forming structures such as stress fibers. The intermediate
filaments extend across the cytoplasm and give mechanical strength to the cell.
5. Answer: FTTF
Difficulty: 2
Section: Function and Origin of the Cytoskeleton
Feedback: Actin and tubulin are globular proteins capable of nucleotide triphosphate
binding and hydrolysis and are found in all eukaryotes. The intermediate filaments, on
 the other hand, are made of filamentous subunits and are not as well conserved. Their
thickness is intermediate between that of the other two cytoskeletal filaments.
6. Answer: protofilaments
Difficulty: 1
Section: Function and Origin of the Cytoskeleton
Feedback: Single microtubules are normally composed of 13 protofilaments—linear
strings of tubulin subunits joined end-to-end.
7. Answer: MIMI
Difficulty: 2
Section: Function and Origin of the Cytoskeleton
Feedback: Microtubules form hollow tubes whose walls are composed of tubulin
subunits. Tubulins can bind GTP. Intermediate filament subunits form α-helical coiled-
coils. These filaments form strong ropelike structures that tolerate mechanical stress, such
as stretching and bending, to a greater extent compared to actin filaments and
microtubules.
8. Answer: D
Difficulty: 2
Section: Function and Origin of the Cytoskeleton
Feedback: Bacteria contain homologs of all three types of cytoskeletal filaments. These
homologs are more diverse than their eukaryotic versions in terms of functional and
structural features.
9. Answer: D
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: A bundle formed from several cross-linked actin filaments has a higher
persistence length than each individual filament. Microtubules have a higher persistence
length compared to actin filaments.
10. Answer: D
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: Since the polymerization rate is higher at the plus (barbed) end, the fluorescent
segments at this end are longer than those at the minus (pointed) end. Both ends have
grown (at different rates), which means the subunit concentration has been above the
critical concentration.
11. Answer: E
Difficulty: 3
 Section: Actin and Actin-binding Proteins
Feedback: The protofilaments cross over approximately every 36 nm (i.e. 13 subunits ×
2.8 nm/subunit), which means a processive myosin of this step size does not have to
rotate around the filament as it moves along it. If the step size was not a multiple of the
helical repeat, carrying large cargoes would involve a screw motion and be less efficient.
12. Answer: A
Difficulty: 2
Section: Actin and Actin-binding Proteins
Feedback: The lag phase corresponds to the rate-limiting nucleation step. If this step is
bypassed by introduction of preformed filament seeds, the lag phase disappears.
13. Answer: D
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: The condition corresponding to curve (2) has a higher koff and hence a higher
Cc, manifested as a lower steady-state percentage of incorporated subunits, as well as an
overall lower net polymerization rate before reaching the steady state.
14. Answer: D
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: Cc = koff/kon. At concentrations of monomers C > Cc, the free-energy change
for polymerization is negative and growth can proceed spontaneously.
15. Answer: D
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: The plus end (right) has higher polymerization rate constants. It also has a
lower Cc value (i.e. a lower koff/kon ratio). ATP-bound actin (B and C) has the higher
tendency for polymerization at both ends.
16. Answer: A
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: The elongation rate (R) at each subunit concentration (C) follows the linear
equation R = kon × C – koff , in which kon represents the slope.
17. Answer: B
Difficulty: 3
Section: Actin and Actin-binding Proteins
 Feedback: The line with the greater slope corresponds to polymerization or
depolymerization at the plus end. Within the treadmilling range (concentrations between
A and E), when the positive elongation rate at the plus end exactly cancels out the
negative rate at the minus end, the length of the filament remains constant. This does not
happen when the monomer concentration (C) is exactly in the middle of the range (since
the two lines have different slopes), but occurs around B for which the sum of the
elongation rates for plus and minus ends equals zero.
18. Answer: E
Difficulty: 2
Section: Actin and Actin-binding Proteins
Feedback: These drugs, whether they stabilize or destabilize the cytoskeletal filaments,
interfere with the dynamics of the cytoskeleton and are therefore cytotoxic.
19. Answer: B
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: Profilin competes with thymosin for the binding of actin subunits, but unlike
thymosin, it does not prevent polymerization. Recruitment of profilin–actin therefore
facilitates the rapid formin-mediated actin polymerization.
20. Answer: E
Difficulty: 1
Section: Actin and Actin-binding Proteins
Feedback: Arp2 and Arp3 are actin homologs in the Arp 2/3 complex, which nucleates
actin filaments by taking advantage of the structural similarities between these molecules
and the actin subunits. MreB and ParM are bacterial actin homologs.
21. Answer: E
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: Both formin and CapZ bind to the plus end and have incompatible functions.
22. Answer: D
Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: With pure subunits, the (dashed) line represents the overall growth rate (i.e. at
both ends) of the actin filaments. Addition of a plus-end capping protein suppresses the
contribution of the plus end to the overall growth, leading to a slower growth and a
higher overall Cc that is close to that of the minus end.
23. Answer: 42351
 Difficulty: 3
Section: Actin and Actin-binding Proteins
Feedback: Tropomyosin binds to several adjacent actin subunits along the actin filament
and stabilizes the filament. α-Actinin cross-links actin filaments, commonly in an
antiparallel fashion. The Arp 2/3 complex nucleates actin filaments and can remain
bound at the minus end. CapZ binds to the plus end and prevents polymerization. The
myosin motor moves on the actin filament.
24. Answer: B
Difficulty: 2
Section: Actin and Actin-binding Proteins
Feedback: Cofilin induces twisting of older actin filaments and destabilizes them. ATP
hydrolysis by incorporated actin is usually slower than filament assembly; therefore the
new actin filaments in the cell are more resistant to depolymerization brought about by
cofilin.
25. Answer: C
Difficulty: 2
Section: Actin and Actin-binding Proteins
Feedback: The tight packing caused by the small bundling protein fimbrin apparently
excludes myosin II from the bundle.
26. Answer: D
Difficulty: 1
Section: Actin and Actin-binding Proteins
Feedback: The Arp 2/3 complex creates a branched network of actin filaments and helps
establish the structure of lamellipodia.
27. Answer: A
Difficulty: 1
Section: Actin and Actin-binding Proteins
Feedback: Spectrin is a long and flexible protein complex in which the two binding sites
for actin are about 200 nm apart. This distance is about an order of magnitude greater
than that of the other proteins listed.
28. Answer: E
Difficulty: 1
Section: Actin and Actin-binding Proteins
Feedback: Proteins of the ERM family play crucial roles including connecting the cortical
actin cytoskeleton to the plasma membrane and to signaling proteins.
29. Answer: FFFF
 Difficulty: 1
Section: Actin and Actin-binding Proteins
Feedback: The bacterium recruits and activates the Arp 2/3 complex at its surface. The
force generated by actin polymerization at the plus end pushes the bacterium, while
cofilin and capping protein ensure continuous motion and prevent the depletion of free
actin subunits by promoting filament turnover.
30. Answer: FFFFT
Difficulty: 1
Section: Microtubules
Feedback: Both plus-end directed and minus-end directed myosins and kinesins have
been identified; however, all known dyneins move toward the minus end of microtubules.
31. Answer: C
Difficulty: 3
Section: Myosin and Actin
Feedback: Gliding occurs due to many individual steps taken by bound myosin heads in
the presence of ATP. Since myosin II moves toward the plus end of actin filaments and is
immobilized on the glass slide, the actin filaments will glide toward their minus end.
32. Answer: DCAB
Difficulty: 2
Section: Myosin and Actin
Feedback: This sequence of events moves the head on the actin filament.
33. Answer: A
Difficulty: 3
Section: Myosin and Actin
Feedback: The power stroke and tight binding to the actin filament require ATP
hydrolysis and inorganic phosphate (Pi) release. However, the release of myosin from the
actin filament only requires ATP binding.
34. Answer: C
Difficulty: 3
Section: Myosin and Actin
Feedback: Rigor mortis occurs after death due to the availability of myosin binding sites
on actin as a result of elevated Ca2+. Myosins remain attached to actin once they bind and
contract the sarcomeres.
35. Answer: 36%
Difficulty: 3
Section: Myosin and Actin
 Feedback: The work performed by one myosin head in each cycle is:
W = F × d = 3 pN × 10 nm = 3 × 10–20 N.m = 3 × 10–20 J
Multiplying this by Avogadro’s number gives 1.8 × 104 J/mol, which is equivalent to
36% of the free-energy change of ATP hydrolysis.
36. Answer: A
Difficulty: 2
Section: Myosin and Actin
Feedback: The dark band represents the thick myosin filaments and its length remains
fairly constant, whereas the light band and the total sarcomere length shorten by several
percent.
37. Answer: DF
Difficulty: 2
Section: Myosin and Actin
Feedback: The filament sliding and calcium-ion pumping carried out by these two
ATPases require a large supply of ATP in these cells.
38. Answer: I
Difficulty: 3
Section: Myosin and Actin
Feedback: Increased sensitivity to Ca2+ may result in hypertrophy by increasing cardiac
muscle contraction, which can be counteracted by drugs that block calcium channels thus
reducing the concentration of calcium available to the troponin complex.
39. Answer: DEACB
Difficulty: 2
Section: Myosin and Actin
Feedback: This sequence of events results in a slow but sustained contraction in smooth
muscle cells.
40. Answer: E
Difficulty: 1
Section: Myosin and Actin
Feedback: The troponin complex regulates the contraction of sarcomeres in skeletal and
heart muscle cells. Non-muscle contractile bundles are regulated by myosin
phosphorylation.
41. Answer: E
Difficulty: 2
Section: Myosin and Actin
 Feedback: The result shows that the unique insert is necessary for the minus-end
directionality of myosin VI, but not necessary for its motor activity. The experiment does
not address the sufficiency of the insert.
42. Answer: C
Difficulty: 3
Section: Myosin and Actin
Feedback: Myosin V is a processive motor and, not surprisingly, its duty ratio is
significantly higher than that of myosin II. This is consistent with ADP release or ATP
binding being slow (and rate-limiting) in the myosin V cycle, making the motor stay
longer in the attached post-stroke state. In myosin II, inorganic phosphate (Pi) release is
rate-limiting instead, keeping the motor in the released or cocked state for a longer
fraction of the cycle.
43. Answer: A
Difficulty: 3
Section: Microtubules
Feedback: Thirteen protofilaments have a total of thirteen staggers between them. Thus, a
full turn of the helix has a rise of approximately 12 nm (= 13 staggers × 0.9 nm/stagger).
Since there is a seam, this rise should correspond to an odd number of monomer
distances, i.e. 1, 3, 5, etc. In reality, the number is 3, equivalent to an axial tubulin
displacement of 4 nm (= 12 nm/3).
44. Answer: D
Difficulty: 2
Section: Microtubules
Feedback: Catastrophe is the transition from growth to shrinkage, while rescue is the
transition from shrinkage to growth. The transition frequencies are generally higher in
more dynamic microtubules, which also tend to be shorter.
45. Answer: C
Difficulty: 2
Section: Microtubules
Feedback: Without a GTP cap, shrinking microtubules have curved protofilaments at
their plus ends with weak lateral interactions. Rescue can also happen randomly without
the help of any associated protein.
46. Answer: A
Difficulty: 2
Section: Microtubules
 Feedback: They both nucleate the filaments and remain bound to the minus end. They
also both employ homologs of the filament subunits to catalyze nucleation.
47. Answer: B
Difficulty: 1
Section: Microtubules
Feedback: The centrosome is the major microtubule-organizing center (MTOC) in most
animal cells. The γ-tubulin ring complexes associated with the centrosome nucleate
microtubules that emanate from the center of the cell toward its periphery.
48. Answer: B
Difficulty: 1
Section: Microtubules
Feedback: XMAP215 behaves as a plus-end tracking protein (+TIP), and stabilizes the
microtubules by binding near the plus end and lowering catastrophe frequency.
49. Answer: 4321
Difficulty: 1
Section: Microtubules
Feedback: Kinesin-1, also called the “conventional kinesin”, is a plus-end directed
microtubule motor. Katanin, named after the Japanese word for “sword” is an ATP-
dependent microtubule-severing protein. EB1 and kinesin-13 are +TIPs. The latter also
acts as a catastrophe factor.
50. Answer: DDDMD
Difficulty: 2
Section: Microtubules
Feedback: Dyneins are fast, minus-end directed, microtubule-based motors that have
large structures unrelated to those of kinesins (also microtubule-based) and myosins
(actin-based) and are also faster than these other two motor proteins.
51. Answer: A
Difficulty: 2
Section: Microtubules
Feedback: In the mechanochemical cycle of kinesins, an ATP-bound head binds tightly to
its microtubule track. Myosins release their actin filament once bound to ATP.
52. Answer: 1750 km/h
Difficulty: 3
Section: Microtubules
Feedback: The step frequency of kinesin-1 is about 125 steps per second [= (1000
nm/sec)/(8 nm/step)], while that of a runner is only about 3 steps per second [= (180
 steps/min)/(60 sec/min)]. If the runner had the step frequency of the kinesin motor, they
could run at 1750 km/h (= 42 km/h × 125/3). This is a supersonic speed, faster than
bullets and regular passenger planes.
53. Answer: B
Difficulty: 2
Section: Microtubules
Feedback: Cytoplasmic dyneins rely on the dynactin complex to associate with their
cargoes, including the Golgi components, which are held near the center of the cell by the
action of these motors.
54. Answer: C
Difficulty: 2
Section: Microtubules
Feedback: In this graph, the traces with a negative slope and indicated by thicker lines
represent anterograde movement toward the axon terminal mediated by kinesins; those
traces with a positive slope represent retrograde motion mediated by dynein. The speed is
inversely related to the slope in this graph, and is higher for the retrograde movement.
55. Answer: C
Difficulty: 2
Section: Microtubules
Feedback: Kinesins normally carry out the outward transport of melanosomes toward the
plus end of microtubules at the cell periphery, by winning a tug-of-war against dyneins
that would otherwise transport the pigments back to the center of the cell. The headless
mutant inhibits kinesin, resulting in inhibition of the outward movement.
56. Answer: TFFTF
Difficulty: 2
Section: Microtubules
Feedback: Essentially all microtubules in axons are oriented with their plus end pointed
at the axon terminal. Anterograde movements on these microtubules are exclusive to
kinesins. In dendrites, however, the microtubules are of mixed polarity. The microtubules
are too short to span the entire length of axons or even dendrites.
57. Answer: CCBC
Difficulty: 2
Section: Microtubules
Feedback: Cilia are found in large numbers on ciliated cells such as those lining our
respiratory tract. They are relatively short and beat with a whiplike motion. Axoneme
constitutes the structural core of both cilia and flagella.
58. Answer: B
Difficulty: 2
Section: Microtubules
Feedback: The dynein tail domain is bound to the A microtubule of one doublet, while
the motor domain interacts with the B microtubule of the neighboring doublet. The
former doublet is pushed toward its minus end (and the base of the flagellum) by the
minus-end directed movement of the motor domain on the latter doublet. Proteins like
nexin prevent such sliding, directing the force into a bending motion.
59. Answer: TFTT
Difficulty: 2
Section: Microtubules
Feedback: Primary cilia are nonmotile interphase structures with a very widespread
distribution among various cells. They are thought to have sensory and signaling
functions.
60. Answer: III
Difficulty: 2
Section: Intermediate Filaments and Septins
Feedback: The highly resilient intermediate filaments have smaller persistence length
compared to other cytoskeletal filaments, and are not polar.
61. Answer: B
Difficulty: 1
Section: Intermediate Filaments and Septins
Feedback: Keratins give cells mechanical strength, and provide tough coverings for
animals. Every keratin filament is composed of an equal mix of type I (acidic) and type II
(neutral/basic) keratins. These filaments are also involved in anchoring the cell
cytoskeleton at desmosomes and hemidesmosomes.
62. Answer: D
Difficulty: 1
Section: Intermediate Filaments and Septins
Feedback: Cell rupture caused by mechanical trauma, and disorganization or clumping of
the keratin filaments, is the hallmark of diseases (such as cornea diseases and skin
blistering) caused by mutations in keratins and their associated proteins.
63. Answer: C
Difficulty: 1
Section: Intermediate Filaments and Septins
 Feedback: Both of these filament types are found in an axon and are critical for its
structure and function.
64. Answer: E
Difficulty: 1
Section: Intermediate Filaments and Septins
Feedback: They are septins.
65. Answer: E
Difficulty: 2
Section: Intermediate Filaments and Septins
Feedback: SUN proteins in the inner nuclear membrane bind to KASH proteins in the
outer nuclear membranes. Through this interaction, nuclear lamina and chromosomes
(which bind to SUN proteins) are connected to actin filaments, microtubule motors, or
plectins (which bind to KASH proteins) in the cytoplasm.
66. Answer: E
Difficulty: 1
Section: Cell Polarization and Migration
Feedback: Sperm cell motility is achieved through flagellum-mediated swimming.
67. Answer: 1321
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: Filopodia and stress fibers are linear structures, lamellipodia form flat, cross-
linked networks, while invadopodia protrude across tissue barriers as footlike protrusions.
68. Answer: D
Difficulty: 1
Section: Cell Polarization and Migration
Feedback: Blebbing is mostly observed in vivo where the substratum is pliable. Both
lamellipodia formation and blebbing require the activity of myosin II at some point. One
of the key differences between the two is in their requirements for membrane interaction
with cortical actin filaments.
69. Answer: D
Difficulty: 3
Section: Cell Polarization and Migration
Feedback: The actin filaments at the leading edge form a web, the whole of which
undergoes treadmilling. An incorporated actin in this web remains more or less immobile
relative to the substratum, but is constantly moving away from the polymerizing plus end
(and the membrane) and getting closer to the depolymerizing minus end.
70. Answer: C
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: The lamellipodium forms at the front of the cell toward where it is migrating.
The cell is about 20 µm across and can move as fast as 30 µm/sec.
71. Answer: D
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: With the loss of the stress fibers and focal adhesions as a result of the
depletion of the myosin isoform, the traction forces on the substratum are expected to
decrease compared to normal cells.
72. Answer: D
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: The Arp 2/3 complex nucleates a two-dimensional web of actin filaments in a
lamellipodium. Behind the leading edge, cofilin disassembles older filaments which
contain ADP-actin.
73. Answer: HCH
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: The Rho family proteins regulate the actin cytoskeleton and cell polarization
in different ways by acting on different but overlapping sets of target proteins.
74. Answer: C
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: At the front of the cell (toward the source of the bacterial peptides), the Rac
pathway dominates and limits the activity of the Rho GTPase to the other end of the cell.
75. Answer: BADC
Difficulty: 2
Section: Cell Polarization and Migration
Feedback: Rac-GTP (B) promotes lamellipodium formation (D) by activating WASp
family members, which leads to the nucleation of branched actin networks by the Arp 2/3
complex, as well as by activating filamin, a gel-forming actin cross-linker. Rho-GTP (A),
on the other hand, activates formin to create parallel actin bundles, inhibits cofilin to
stabilize actin filaments, and increases myosin motor activity, which all lead to formation
of more stress fibers (C).