paper two

3.5.1 Compare the structure of DNA and RNA

3.5.2 Outline DNA transcription in terms of the formation of an RNA strand
complementary to the DNA strand by RNA polymerase
Transcription is the process by which an RNA sequence is produced from a
DNA template:
RNA polymerase separates the DNA strands and synthesises a
complementary RNA copy from one of the DNA strands
It does this by covalently bonding ribonucleoside triphosphates that align
opposite their exposed complementary partner (using the energy from the
cleavage of the additional phosphate groups to join them together)
Once the RNA sequence has been synthesised, RNA polymerase will detach
from the DNA molecule and the double helix will reform
The sequence of DNA that is transcribed into RNA is called a gene
Transcription occurs in the nucleus (where the DNA is) and, once made, the
mRNA moves to the cytoplasm (where translation can occur)
Three main types of RNA are predominantly made:
Messenger RNA (mRNA): A transcript copy of a gene used to encode a
polypeptide
Transfer RNA (tRNA): A clover leaf shaped sequence that carries an amino
acid
Ribosomal RNA (rRNA): A primary component of ribosomes
3.5.3 Describe the genetic code in terms of codons comprised of triplets of
bases
The genetic code is the set of rules by which information encoded in mRNA
sequences is converted into proteins (amino acid sequences) by living cells
Codons are a triplet of bases which encodes a particular amino acid
As there are four bases, there are 64 different codon combinations (4 x 4 x 4
= 64)
The order of the codons determines the amino acid sequence for a protein
The coding region always starts with a START codon (AUG) and terminates
with a STOP codon

The Genetic Code

The genetic code has the following features:
It is universal - every living thing uses the same code (there are only a few
rare and minor exceptions)
It is degenerate - there are only 20 amino acids but 64 codons, so more than
one codon may code for the same amino acid (this allows for silent mutations
whereby a change in the DNA sequence does not affect the polypeptide
sequence)
3.5.4 Explain the process of translation, leading to polypeptide formation
Translation is the process of protein synthesis in which the genetic
information encoded in mRNA is translated into a sequence of amino acids in
a polypeptide chain
Ribosomes bind to mRNA in the cell's cytoplasm and move along the mRNA
molecule in a 5' - 3' direction until it reaches a start codon (AUG)
Anticodons on tRNA molecules align opposite appropriate codons according
to complementary base pairing (e.g. UAC will align with AUG)
Each tRNA molecule carries a specific amino acid (according to the genetic
code)
Ribosomes catalyse the formation of peptide bonds between adjacent amino
acids (via a condensation reaction)
The ribosome moves along the mRNA molecule synthesising a polypeptide
chain until it reaches a stop codon, at this point translation stops and the
polypeptide chain is released
The Process of Translation
3.5.5 Explain the relationship between one gene and one polypeptide
A gene is a sequence of DNA which encodes a polypeptide sequence
A gene sequence is converted into a polypeptide sequence via the processes
of transcription (making an mRNA transcript) and translation (polypeptide
synthesis)
Translation uses tRNA molecules and ribosomes to join amino acids into a
polypeptide chain according to the mRNA sequence (as read in codons)

The universality of the genetic code means all organisms show the same
relationship between genes and polypeptides (indicating a common ancestry
and allowing for transgenic techniques to be employed)
Some proteins may consist of a number of polypeptide chains and thus need
multiple genes (e.g. haemoglobin consists of four polypeptide subunits
encoded by two different genes)
When a gene is mutated it may lead to the synthesis of a defective
polypeptide, hence affecting protein function
The 'One Gene - One Polypeptide' Rule
There are two exceptions to the 'one gene - one polypeptide' rule:
Genes encoding for tRNA and rRNA do not code for polypeptide sequences
(only mRNA sequences code for polypeptides)
A single gene may code for multiple polypeptides if alternative splicing
occurs (the removal of exons as well as introns)
Transcription & translation
3.5.1 Compare the structure of RNA and DNA.

DNA and RNA both consist of nucleotides which contain a sugar, a base and a
phosphate group. However there are a few differences. Firstly, DNA is
composed of a double strand forming a helix whereas RNA is only composed
of one strand. Also the sugar in DNA is deoxyribose whereas in RNA it is
ribose. Finally, both DNA and RNA have the bases adenine, guanine and
cytosine. However DNA also contains thymine which is replaced by uracil in
RNA.
3.5.2 Outline DNA transcription in terms of the formation of an RNA strand
complementary to tTranscription & translation
3.5.1 Compare the structure of RNA and DNA.

DNA and RNA both consist of nucleotides which contain a sugar, a base and a
phosphate group. However there are a few differences. Firstly, DNA is
composed of a double strand forming a helix whereas RNA is only composed
of one strand. Also the sugar in DNA is deoxyribose whereas in RNA it is
ribose. Finally, both DNA and RNA have the bases adenine, guanine and
cytosine. However DNA also contains thymine which is replaced by uracil in

RNA.

3.5.2 Outline DNA transcription in terms of the formation of an RNA strand

complementary to the DNA strand by RNA polymerase.
DNA transcription is the formation of an RNA strand which is complementary
to the DNA strand. The first stage of transcription is the uncoiling of the DNA
double helix. Then, the free RNA nucleotides start to form an RNA strand by
using one of the DNA strands as a template. This is done through
complementary base pairing, however in the RNA chain, the base thymine is
replaced by uracil. RNA polymerase is the enzyme involved in the formation
of the RNA strand and the uncoiling of the double helix. The RNA strand then
elongates and then separates from the DNA template. The DNA strands then
reform a double helix. The strand of RNA formed is called messenger RNA.
3.5.3 Describe the genetic code in terms of codons composed of triplets of
bases.
A triplet of bases (3 bases) forms a codon. Each codon codes for a particular
amino acid. Amino acids in turn link to form proteins. Therefore DNA and RNA
regulate protein synthesis. The genetic code is the codons within DNA and
RNA, composed of triplets of bases which eventually lead to protein
synthesis.
3.5.4 Explain the process of translation, leading to polypeptide formation.
Translation is the process through which proteins are synthesized. It uses
ribosomes, messenger RNA which is composed of codons and transfer RNA
which has a triplet of bases called the anticodon. The first stage of translation
is the binding of messenger RNA to the small subunit of the ribosome. The
transfer RNAs have a specific amino acid attached to them which
corresponds to their anticodons. A transfer RNA molecule will bind to the
ribosome however its anticodon must match the codon on the messenger
RNA. This is done through complementary base pairing. These two form a
hydrogen bond together. Another transfer RNA molecule then bonds. Two
transfer RNA molecules can bind at once. Then the two amino acids on the
two transfer RNA molecules form a peptide bond. The first transfer RNA then
detaches from the ribosome and the second one takes its place.The
ribosome moves along the messenger RNA to the next codon so that another
transfer RNA can bind. Again, a peptide bond is formed between the amino
acids and this process continues. This forms a polypeptide chain and is the
basis of protein synthesis.
3.5.5 Discuss the relationship between one gene and one polypeptide.

A polypeptide is formed by amino acids liking together through peptide

bonds. There are 20 different amino acids so a wide range of polypeptides are
possible. Genes store the information required for making polypeptides. The
information is stored in a coded form by the use of triplets of bases which
form codons. The sequence of bases in a gene codes for the sequence of
amino acids in a polypeptide. The information in the genes is decoded during
transcription and translation leading to protein synthesis.e DNA strand by
RNA polymerase.
DNA transcription is the formation of an RNA strand which is complementary
to the DNA strand. The first stage of transcription is the uncoiling of the DNA
double helix. Then, the free RNA nucleotides start to form an RNA strand by
using one of the DNA strands as a template. This is done through
complementary base pairing, however in the RNA chain, the base thymine is
replaced by uracil. RNA polymerase is the enzyme involved in the formation
of the RNA strand and the uncoiling of the double helix. The RNA strand then
elongates and then separates from the DNA template. The DNA strands then
reform a double helix. The strand of RNA formed is called messenger RNA.
3.5.3 Describe the genetic code in terms of codons composed of triplets of
bases.
A triplet of bases (3 bases) forms a codon. Each codon codes for a particular
amino acid. Amino acids in turn link to form proteins. Therefore DNA and RNA
regulate protein synthesis. The genetic code is the codons within DNA and
RNA, composed of triplets of bases which eventually lead to protein
synthesis.
3.5.4 Explain the process of translation, leading to polypeptide formation.
Translation is the process through which proteins are synthesized. It uses
ribosomes, messenger RNA which is composed of codons and transfer RNA
which has a triplet of bases called the anticodon. The first stage of translation
is the binding of messenger RNA to the small subunit of the ribosome. The
transfer RNAs have a specific amino acid attached to them which
corresponds to their anticodons. A transfer RNA molecule will bind to the
ribosome however its anticodon must match the codon on the messenger
RNA. This is done through complementary base pairing. These two form a
hydrogen bond together. Another transfer RNA molecule then bonds. Two
transfer RNA molecules can bind at once. Then the two amino acids on the
two transfer RNA molecules form a peptide bond. The first transfer RNA then
detaches from the ribosome and the second one takes its place.The
ribosome moves along the messenger RNA to the next codon so that another
transfer RNA can bind. Again, a peptide bond is formed between the amino
acids and this process continues. This forms a polypeptide chain and is the

basis of protein synthesis.

3.5.5 Discuss the relationship between one gene and one polypeptide.
A polypeptide is formed by amino acids liking together through peptide
bonds. There are 20 different amino acids so a wide range of polypeptides are
possible. Genes store the information required for making polypeptides. The
information is stored in a coded form by the use of triplets of bases which
form codons. The sequence of bases in a gene codes for the sequence of
amino acids in a polypeptide. The information in the genes is decoded during
transcription and translation leading to protein synthesis.

Movement Through the Plasma Membrane

Substances that must be able to enter a cell are water, oxygen, and
nutrients. On TV medical dramas, you'll often see technicians administering a
saline drip to a patient who has lost blood or is dehydrated. This saline
solution maintains a specific concentration of dissolved substances in the
blood and body fluids. When dehydrated, our concentration of dissolved
substances increases, upsetting the balance in our cells. Water can freely
move in and out of cells to maintain the same water pressure on both sides of
the plasma membrane. Oxygen is important because cells are undergoing
cellular respiration. A cell takes chemical bond energy and converts it to a
form of energy that it can use--a molecule of ATP. ATP contains small amounts
of energy appropriate to powering cellular processes. This process of energy
conversion requires oxygen (we will discuss this in more detail in Lesson 4).
For aerobic cellular respiration to occur inside this cell, oxygen must move
through the plasma membrane.

Some nutrients enter freely; others are controlled. Cells must also export the
products that they make. (We'll discuss how cells make proteins in Lesson 7.)
The cells in your liver are amazing: they make many, many proteins that
leave the liver cells to be transported to cells in other parts of your body.
Waste products must also leave a cell. For instance, during cellular
respiration, carbon dioxide is released as a waste product. It goes back into
our blood stream and eventually is exhaled from our lungs. So cells must
interact with their environment yet maintain fairly constant internal
conditions. There are three ways that substances move across the plasma
membrane: (1) diffusion, (2) facilitated diffusion, and (3) active transport.

Diffusion
The simplest method of moving substances across the membrane is diffusion,
the random movement of particles from an area of higher concentration to an
area of lower concentration. Diffusion follows a concentration gradient (Figure
3.4) and will occur across the plasma membrane as long as there is no
restriction (e.g., size or charge of molecule). Non-polar lipids and small
molecules such as oxygen and carbon dioxide are able to pass freely through
the membrane. For example, because oxygen is used for cellular respiration,
there is always a higher oxygen concentration outside the cell and a lower
concentration inside. As oxygen follows this gradient from higher to lower
concentration, oxygen molecules are always diffusing into the cell. Carbon
dioxide also undergoes diffusion but in the opposite direction because there is
always a higher concentration of carbon dioxide inside than outside the cell.
Other small molecules, like ethanol, also can diffuse freely through the
plasma membrane, which is why alcohol hits your system fairly quickly: it
diffuses from your digestive system into your bloodstream and then is carried
to all of your cells. It affects these fairly rapidly and evenly, diffusing into
them until the cellular concentration is approximately equal to that in your
bloodstream. Diffusion does not require the input of energy on the part of the
cell.

Graphic showing the diffusion of a lump of sugar in four steps: Step 1, the
sugar is dropped into a beaker of water; Step 2, the sugar molecules beging
to spread throughout the water; Steps 3 and 4, the sugar molecules continue
to spread out in the water.

Figure 3.4. Diffusion of Sugar in Water

The McGraw-Hill Companies, Inc. Permission granted for reproduction

Osmosis
Osmosis is the term for a special type of diffusion, the diffusion of water, and
is based on the concentration of dissolved substances (solutes), either in the
fluid within the cell or in your blood stream, which cannot cross the
membrane. In the figure below (Figure 3.5), a beaker is shown to demonstrate

the movement of water within a cell by osmosis.

Water molecules, which can cross the membrane, will diffuse to the side with
the lower water concentration (higher solute concentration). The first frame is
isotonic, meaning the water molecules are evenly distributed between the
two sides of the beaker. In the center frame, you add a nondiffusible solute to
the right side. With the addition of these molecules, there is less water
pressure, so water will flow from the left side of the beaker to the right, until
the water pressure is equal on both sides, illustrated by the third frame.
Water will move into your cells or out of your cells depending upon the
concentration of solutes, like salt, in your body tissues and in your blood
stream. Therefore, fluid replacement for an injured person must match the
bloodstream's dissolved solute concentration, as is true of isotonic saline,
which will not cause water to leave or enter cells too rapidly. Although the
movement of water is given a special name, osmosis follows a concentration
gradient (its own) and does not require the input of energy.

Graphic depicting osmosis. In step 1 a permeable membrane in a beaker of

water causes water to distribute equally on either side of the membrane. In
step 2, solute molecules that cannot cross the membrane at added to one
side of the beaker. The water molecules on the solute side bind to the solute
which decreases the number of water molecules on that side. In step 3,
diffusion causes the free water molecules on the non-solute side to move to
the solute side.

Figure 3.5. Movment of Water by Osmosis

The McGraw-Hill Companies, Inc. Permission granted for reproduction

Facilitated Diffusion
Many substances will follow a concentration gradient, but are too large to get
through the membrane on their own. These substances need some kind of
carrier molecule to help them. They must move through a protein that is
imbedded in the plasma membrane. In the process of cellular respiration, we
take chemical bond energy and turn it into a form of energy that the cells can
use. One of the molecules whose chemical bonds are broken down is glucose.
For example, when you eat a potato, which contains lots of starch, as it goes
through your digestion system, the polymers of starch are broken down into

glucose monomers in your small intestine, then glucose is absorbed across

the small intestine and goes into your blood stream. That glucose is used by
all of the cells in your body to provide energy. The concentration of glucose is
usually higher outside a cell than it is inside, because once it enters the cell it
is broken down. So, you have a concentration gradient, but glucose is too big
to move freely through the membrane. There are carrier molecules in the cell
membrane that are specific to glucose. They do not allow other molecules
through. There are other carrier proteins for molecules such as amino acids.
This is part of the complexity of cell membranes, because you have to have
different carrier molecules for different substances that are going to be
brought into or excreted from the cell. See Figure 3.6 for an illustration of
facilitated diffusion.
Proteins in the plasma membrane act as gates to allow movement of large
molecules into and out of a cell. In step 1, a molecule binds a particular
protein that is embedded in the plasma membrane. In step 2, the protein
helps or facilitates the movement of the molecule through the plasma
membrane. In step 3, the molecule is released on the other side of the
membrane. The same protein will move the molecule in either direction, and
this type of movement across the plasma membrane does not require energy.
Figure 3.6. The Movement of a Substance Through the Plasma Membrane
Using a Carrier Molecule
The McGraw-Hill Companies, Inc. Permission granted for reproduction
Active Transport
The last type of general mechanism that cells use to transport materials is
more complicated because it requires the cells to expend energy. That is why
it is called active transport. In this case, substances are not going to go with
the concentration gradient, they're actually going against the concentration
gradient. When substances are going against their gradient, energy must be
used. We call these proteins where this energy is used pumps because they
are pumping substances against the concentration gradient. There are many
different pumps for different molecules; one that has been well-studied is the
sodium-potassium pump.

Sodium and potassium are extremely important molecules, particularly in

animals. In our nervous system, the balance between these two ions, sodium
and potassium, allows the transmission of nerve impulses. For instance, if I
think that I am going to move my hand, it is the gradient created by this
pump that causes the message to be propagated down a nerve, allowing my
hand to move. So this is an extremely important pump. It has been estimated

that about 30 percent of the energy in our cells is used to maintain the
concentration of sodium against its gradient. Normally, there is more sodium
inside of a cell than outside. A transport protein in the membrane has specific
receptors for sodium ions. Sodium ions inside the cell attach to these
proteins, as do ATP molecules which are the energy currency of the cells.
When the ATP molecule splits, it provides energy to change the shape of the
protein channel. When the protein changes shape, it traps the sodium ions
and they are pushed to the other side of the membrane (see Figure 3.7).
Proteins in the plasma membrane act as gates to allow movement of large
molecules into and out of a cell. In step 1, a molecule binds a particular
protein that is embedded in the plasma membrane. In step 2, the protein
helps or facilitates the movement of the molecule through the plasma
membrane. In step 3, the molecule is released on the other side of the
membrane. The same protein will move the molecule in either direction, and
this type of movement across the plasma membrane does not require energy.

Figure 3.7. The Sodium-Potassium Pump

The McGraw-Hill Companies, Inc. Permission granted for reproduction
On the outside of the membrane, two potassium ions bind and are then
transported to the inside of the cell. This creates a concentration gradient
with the higher concentration of sodium outside the cell, and potassium
inside the cell.
This concentration gradient is also used to help bring other substances into
the cell against their concentration gradients, through coupled channels
(Figure 3.8). In this process a facilitated diffusion channel allows the diffusion
of sodium ions back into the cell but only if it is accompanied by another
particular molecule. There are specific coupled channels for many needed
molecules such as sugars and amino acids. For instance, there is a coupled
channel protein that allows diffusion of sodium ions into the cell if it is
coupled to glucose. So when the sodium ions diffused back into the cell, it
"pulls" glucose along into the cell even though it is against the concentration
gradient of the glucose. It is important for the function of the protein channel
to have this high sodium concentration outside of the cell.
These pumps are important to maintaining cellular conditions, allowing a
number of different processes, including transmission of nerve impulses and
transport of nutrients into the cells. The sodium potassium pump is the most
active, but there are many other ions that are pumped in and out of cells to
establish concentration gradients for different reasons. These three methods,
diffusion (including osmosis), facilitated diffusion, and active transport, allow

cells to regulate what can, or cannot, cross the plasma membrane.

Graphic depicts how the sodium-potassium channel is linked to another
protein in the plasma membrane called a coupled channel. The sodiumpotassium pump creates a concentration gradient where there are more
sodium ions outside of the cell. However, these sodium ions can get back
into the cell via the coupled channel as long as the pass through that channel
with another molecule, such as sugar.

The endoplasmic reticulum (ER) is an organelle

found in the cells of eukaryotic organisms. It is
an interconnected network of flattened sacs or
tubes encased in membranes. These
membranes are continuous, joining with the
outer membrane of the nuclear membrane.

The endoplasmic reticulum (ER) is a type of

organelle in the eukaryotic cells that forms an
interconnected network of flattened,
membrane-enclosed sacs or tube-like
structures known as cisternae. The membranes
of the ER are continuous with the outer nuclear
membrane. Endoplasmic reticulum occurs in
most types of eukaryotic cells, including the
most primitive Giardia,[1] but is absent from
red blood cells and spermatozoa. There are two
types of endoplasmic reticulum: rough and
smooth. The outer (cytosolic) face of the rough
endoplasmic reticulum is studded with
ribosomes that are the sites of protein
synthesis. The rough endoplasmic reticulum is

especially prominent in cells such as

hepatocytes. The smooth endoplasmic
reticulum lacks ribosomes and functions in
lipid manufacture and metabolism, the
production of steroid hormones, and
detoxification.[2] The smooth ER is especially
abundant in mammalian liver and gonad cells.
The lacy membranes of the endoplasmic
reticulum were first seen in 1945 using
electron microscopy.

1 Nucleus 2 Nuclear pore 3 Rough

endoplasmic reticulum (RER) 4 Smooth
endoplasmic reticulum (SER) 5 Ribosome on
the rough ER 6 Proteins that are transported
7 Transport vesicle 8 Golgi apparatus 9 Cis
face of the Golgi apparatus 10 Trans face of
the Golgi apparatus 11 Cisternae of the Golgi
apparatus

3D rendering of endoplasmic reticulum

The general structure of the endoplasmic
reticulum is a network of membranes called
cisternae. These sac-like structures are held
together by the cytoskeleton. The phospholipid
membrane encloses the cisternal space (or

lumen), which is continuous with the

perinuclear space but separate from the
cytosol. The functions of the endoplasmic
reticulum can be summarized as the synthesis
and export of proteins and membrane lipids,
but varies between ER and cell type and cell
function. The quantity of both rough and
smooth endoplasmic reticulum in a cell can
slowly interchange from one type to the other,
depending on the changing metabolic activities
of the cell. Transformation can include
embedding of new proteins in membrane as
well as structural changes. Changes in protein
content may occur without noticeable
structural changes.[citation needed]

Rough endoplasmic reticulum[edit]

An animation showing how a protein destined

for the secretory pathway is synthesized into
the rough endoplasmic reticulum (which
appears at upper right in animation when
approximately half of animation is done). The
total animation time is about 2 minutes.
The surface of the rough endoplasmic
reticulum (often abbreviated RER or Rough ER)
(also called ergastoplasm) is studded with
protein-manufacturing ribosomes giving it a

"rough" appearance (hence its name). The

binding site of the ribosome on the rough
endoplasmic reticulum is the translocon.[3]
However, the ribosomes bound to it at any one
time are not a stable part of this organelle's
structure as they are constantly being bound
and released from the membrane. A ribosome
only binds to the RER once a specific proteinnucleic acid complex forms in the cytosol. This
special complex forms when a free ribosome
begins translating the mRNA of a protein
destined for the secretory pathway.[4] The first
5-30 amino acids polymerized encode a signal
peptide, a molecular message that is
recognized and bound by a signal recognition
particle (SRP). Translation pauses and the
ribosome complex binds to the RER translocon
where translation continues with the nascent
protein forming into the RER lumen and/or
membrane. The protein is processed in the ER
lumen by an enzyme (a signal peptidase),
which removes the signal peptide. Ribosomes
at this point may be released back into the
cytosol; however, non-translating ribosomes
are also known to stay associated with
translocons.[5]

The membrane of the rough endoplasmic

reticulum forms large double membrane sheets

that are located near, and continuous with, the

outer layer of the nuclear envelope.[6]
Although there is no continuous membrane
between the endoplasmic reticulum and the
Golgi apparatus, membrane-bound vesicles
shuttle proteins between these two
compartments.[7] Vesicles are surrounded by
coating proteins called COPI and COPII. COPII
targets vesicles to the Golgi apparatus and
COPI marks them to be brought back to the
rough endoplasmic reticulum. The rough
endoplasmic reticulum works in concert with
the Golgi complex to target new proteins to
their proper destinations. A second method of
transport out of the endoplasmic reticulum
involves areas called membrane contact sites,
where the membranes of the endoplasmic
reticulum and other organelles are held closely
together, allowing the transfer of lipids and
other small molecules.[8][9]

The rough endoplasmic reticulum is key in

multiple functions:

Manufacture of lysosomal enzymes with a

mannose-6-phosphate marker added in the cisGolgi network[citation needed]
Manufacture of secreted proteins, either

secreted constitutively with no tag or secreted

in a regulatory manner involving clathrin and
paired basic amino acids in the signal peptide.
Integral membrane proteins that stay
embedded in the membrane as vesicles exit
and bind to new membranes. Rab proteins are
key in targeting the membrane; SNAP and
SNARE proteins are key in the fusion event.
Initial glycosylation as assembly continues.
This is N-linked (O-linking occurs in the Golgi).
N-linked glycosylation: If the protein is
properly folded, Oligosaccharyltransferase
recognizes the AA sequence NXS or NXT (with
the S/T residue phosphorylated) and adds a 14sugar backbone (2-N-acetylglucosamine, 9branching mannose, and 3-glucose at the end)
to the side-chain nitrogen of Asn.
Smooth endoplasmic reticulum[edit]
The smooth endoplasmic reticulum
(abbreviated SER) has functions in several
metabolic processes. It synthesizes lipids,
phospholipids, and steroids. Cells which
secrete these products, such as those in the
testes, ovaries, and sebaceous glands have an
abundance of smooth endoplasmic reticulum.
[10] It also carries out the metabolism of
carbohydrates, detoxification of natural
metabolism products and of alcohol and drugs,

attachment of receptors on cell membrane

proteins, and steroid metabolism.[11] In
muscle cells, it regulates calcium ion
concentration. Smooth endoplasmic reticulum
is found in a variety of cell types (both animal
and plant), and it serves different functions in
each. The smooth endoplasmic reticulum also
contains the enzyme glucose-6-phosphatase,
which converts glucose-6-phosphate to
glucose, a step in gluconeogenesis. It is
connected to the nuclear envelope and
consists of tubules that are located near the
cell periphery. These tubes sometimes branch
forming a network that is reticular in
appearance.[6] In some cells, there are dilated
areas like the sacs of rough endoplasmic
reticulum. The network of smooth endoplasmic
reticulum allows for an increased surface area
to be devoted to the action or storage of key
enzymes and the products of these enzymes.

Sarcoplasmic reticulum[edit]

Skeletal muscle fiber, with sarcoplasmic

reticulum colored in blue.
The sarcoplasmic reticulum (SR), from the
Greek sarx ("flesh"), is smooth ER found
in myocytes. The only structural difference

between this organelle and the smooth

endoplasmic reticulum is the medley of
proteins they have, both bound to their
membranes and drifting within the confines of
their lumens. This fundamental difference is
indicative of their functions: The endoplasmic
reticulum synthesizes molecules, while the
sarcoplasmic reticulum stores calcium ions and
pumps them out into the sarcoplasm when the
muscle fiber is stimulated.[12][13] After their
release from the sarcoplasmic reticulum,
calcium ions interact with contractile proteins
that utilize ATP to shorten the muscle fiber.
The sarcoplasmic reticulum plays a major role
in excitation-contraction coupling.[14]

Functions[edit]
The endoplasmic reticulum serves many
general functions, including the folding of
protein molecules in sacs called cisternae and
the transport of synthesized proteins in
vesicles to the Golgi apparatus. Correct folding
of newly made proteins is made possible by
several endoplasmic reticulum chaperone
proteins, including protein disulfide isomerase
(PDI), ERp29, the Hsp70 family member
BiP/Grp78, calnexin, calreticulin, and the
peptidylpropyl isomerase family. Only properly
folded proteins are transported from the rough

ER to the Golgi apparatus unfolded proteins

cause an unfolded protein response as a stress
response in the ER. Disturbances in redox
regulation, calcium regulation, glucose
deprivation, and viral infection[15] or the overexpression of proteins[16] can lead to
endoplasmic reticulum stress response (ER
stress), a state in which the folding of proteins
slows, leading to an increase in unfolded
proteins. This stress is emerging as a potential
cause of damage in hypoxia/ischemia, insulin
resistance, and other disorders.[17]

The fluid mosaic model explains

various observations regarding the
structure of functional cell membranes. The
model, which was devised by SJ Singer and GL
Nicolson in 1972, describes the cell membrane
as a two-dimensional liquid in which that
restrict the lateral diffusion of membrane
components. Such domains are defined by the
existence of regions within the membrane with
special lipid and protein composition that
promote the formation of lipid rafts or protein
and glycoprotein complexes. Another way to
define membrane domains is the association of
the lipid membrane with the cytoskeleton

filaments and the extracellular matrix through

membrane proteins.[1] The current model
describes important features relevant to many
cellular processes, including: cell-cell
signaling, apoptosis, cell division, membrane
budding, and cell fusion.

A microbody is a type of
organelle that is found in the
cells of plants, protozoa, and animals.
Organelles in the microbody family include
peroxisomes, glyoxysomes, glycosomes and
hydrogenosomes. In vertebrates, microbodies
are especially prevalent in the liver and kidney
organs.

Schematic drawing illustrating

clathrin-mediated (left) and
clathrin-independent
endocytosis (right) of synaptic
vesicle membranes.
Endocytosis pathways can be subdivided into
four categories: namely, receptor-mediated
endocytosis, caveolae, macropinocytosis, and
phagocytosis.[1]

Clathrin-mediated endocytosis is mediated by

small (approx. 100 nm in diameter) vesicles
that have a morphologically characteristic coat
made up of a complex of proteins that are
mainly associated with the cytosolic protein
clathrin. Clathrin-coated vesicles (CCVs) are
found in virtually all cells and form domains of
the plasma membrane termed clathrin-coated
pits. Coated pits can concentrate large
extracellular molecules that have different
receptors responsible for the receptormediated endocytosis of ligands, e.g. low
density lipoprotein, transferrin, growth factors,
antibodies and many others.[2]