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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)

a base and a phosphate group.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.5. DNA is composed of a double strand forming a helix whereas RNA is only composed of one strand. both DNA and RNA have the bases adenine. DNA is composed of a double strand forming a helix whereas RNA is only composed of one strand. both DNA and RNA have the bases adenine. However DNA also contains thymine which is replaced by uracil in . Finally.1 Compare the structure of RNA and DNA.1 Compare the structure of RNA and DNA. Also the sugar in DNA is deoxyribose whereas in RNA it is ribose.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. guanine and cytosine. However DNA also contains thymine which is replaced by uracil in RNA. a base and a phosphate group. DNA and RNA both consist of nucleotides which contain a sugar. 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.5. hence affecting protein function The 'One Gene . DNA and RNA both consist of nucleotides which contain a sugar. Finally.g. guanine and cytosine.One Polypeptide' Rule There are two exceptions to the 'one gene . 3. However there are a few differences.5. Also the sugar in DNA is deoxyribose whereas in RNA it is ribose. Firstly. Firstly.2 Outline DNA transcription in terms of the formation of an RNA strand complementary to tTranscription & translation 3. However there are a few differences.

Then. DNA transcription is the formation of an RNA strand which is complementary to the DNA strand. however in the RNA chain. A triplet of bases (3 bases) forms a codon. It uses ribosomes. This is done through complementary base pairing.5 Discuss the relationship between one gene and one polypeptide. The first stage of transcription is the uncoiling of the DNA double helix. messenger RNA which is composed of codons and transfer RNA which has a triplet of bases called the anticodon. Each codon codes for a particular amino acid. 3. composed of triplets of bases which eventually lead to protein synthesis.RNA. The DNA strands then reform a double helix. This forms a polypeptide chain and is the basis of protein synthesis. A transfer RNA molecule will bind to the ribosome however it’s anticodon must match the codon on the messenger RNA. 3. Then the two amino acids on the two transfer RNA molecules form a peptide bond. a peptide bond is formed between the amino acids and this process continues. Again. The strand of RNA formed is called messenger RNA. This is done through complementary base pairing. The first stage of translation is the binding of messenger RNA to the small subunit of the ribosome. RNA polymerase is the enzyme involved in the formation of the RNA strand and the uncoiling of the double helix. Translation is the process through which proteins are synthesized. 3.4 Explain the process of translation.3 Describe the genetic code in terms of codons composed of triplets of bases. The RNA strand then elongates and then separates from the DNA template.2 Outline DNA transcription in terms of the formation of an RNA strand complementary to the DNA strand by RNA polymerase. Two transfer RNA molecules can bind at once. These two form a hydrogen bond together. . Another transfer RNA molecule then bonds.5.5.The ribosome moves along the messenger RNA to the next codon so that another transfer RNA can bind. the base thymine is replaced by uracil. The genetic code is the codons within DNA and RNA.5.5. the free RNA nucleotides start to form an RNA strand by using one of the DNA strands as a template. Amino acids in turn link to form proteins. leading to polypeptide formation. The transfer RNA’s have a specific amino acid attached to them which corresponds to their anticodons. The first transfer RNA then detaches from the ribosome and the second one takes it’s place. 3. Therefore DNA and RNA regulate protein synthesis.

3 Describe the genetic code in terms of codons composed of triplets of bases. Each codon codes for a particular amino acid. Then the two amino acids on the two transfer RNA molecules form a peptide bond. The strand of RNA formed is called messenger RNA. Again.4 Explain the process of translation. DNA transcription is the formation of an RNA strand which is complementary to the DNA strand. The transfer RNA’s have a specific amino acid attached to them which corresponds to their anticodons. Amino acids in turn link to form proteins. A triplet of bases (3 bases) forms a codon. leading to polypeptide formation. There are 20 different amino acids so a wide range of polypeptides are possible. 3. a peptide bond is formed between the amino acids and this process continues. The first stage of translation is the binding of messenger RNA to the small subunit of the ribosome. Translation is the process through which proteins are synthesized. composed of triplets of bases which eventually lead to protein synthesis. Therefore DNA and RNA regulate protein synthesis. This is done through complementary base pairing. 3.The ribosome moves along the messenger RNA to the next codon so that another transfer RNA can bind.5. Another transfer RNA molecule then bonds. however in the RNA chain. This forms a polypeptide chain and is the . Two transfer RNA molecules can bind at once. The DNA strands then reform a double helix. The RNA strand then elongates and then separates from the DNA template.5. Then. This is done through complementary base pairing. messenger RNA which is composed of codons and transfer RNA which has a triplet of bases called the anticodon. It uses ribosomes. RNA polymerase is the enzyme involved in the formation of the RNA strand and the uncoiling of the double helix. A transfer RNA molecule will bind to the ribosome however it’s anticodon must match the codon on the messenger RNA. The information in the genes is decoded during transcription and translation leading to protein synthesis. The genetic code is the codons within DNA and RNA.A polypeptide is formed by amino acids liking together through peptide bonds. Genes store the information required for making polypeptides.e DNA strand by RNA polymerase. the base thymine is replaced by uracil. The first transfer RNA then detaches from the ribosome and the second one takes it’s place. The sequence of bases in a gene codes for the sequence of amino acids in a polypeptide. The first stage of transcription is the uncoiling of the DNA double helix. The information is stored in a coded form by the use of triplets of bases which form codons. These two form a hydrogen bond together. the free RNA nucleotides start to form an RNA strand by using one of the DNA strands as a template.

The information in the genes is decoded during transcription and translation leading to protein synthesis. Some nutrients enter freely. and nutrients. For aerobic cellular respiration to occur inside this cell. many proteins that leave the liver cells to be transported to cells in other parts of your body. carbon dioxide is released as a waste product. Oxygen is important because cells are undergoing cellular respiration. Cells must also export the products that they make. On TV medical dramas.) The cells in your liver are amazing: they make many. and (3) active transport. (2) facilitated diffusion.basis of protein synthesis. Water can freely move in and out of cells to maintain the same water pressure on both sides of the plasma membrane. It goes back into our blood stream and eventually is exhaled from our lungs. . during cellular respiration. Movement Through the Plasma Membrane Substances that must be able to enter a cell are water. (We'll discuss how cells make proteins in Lesson 7. others are controlled. The information is stored in a coded form by the use of triplets of bases which form codons. There are 20 different amino acids so a wide range of polypeptides are possible. There are three ways that substances move across the plasma membrane: (1) diffusion. A cell takes chemical bond energy and converts it to a form of energy that it can use--a molecule of ATP. 3. Genes store the information required for making polypeptides.5 Discuss the relationship between one gene and one polypeptide. When dehydrated. So cells must interact with their environment yet maintain fairly constant internal conditions. oxygen. oxygen must move through the plasma membrane. ATP contains small amounts of energy appropriate to powering cellular processes. upsetting the balance in our cells. The sequence of bases in a gene codes for the sequence of amino acids in a polypeptide. A polypeptide is formed by amino acids liking together through peptide bonds. Waste products must also leave a cell. For instance. you'll often see technicians administering a saline drip to a patient who has lost blood or is dehydrated. our concentration of dissolved substances increases.5. This process of energy conversion requires oxygen (we will discuss this in more detail in Lesson 4). This saline solution maintains a specific concentration of dissolved substances in the blood and body fluids.

In the figure below (Figure 3. which cannot cross the membrane. Step 2. Diffusion does not require the input of energy on the part of the cell. and is based on the concentration of dissolved substances (solutes). size or charge of molecule). the sugar is dropped into a beaker of water. Diffusion of Sugar in Water ©The McGraw-Hill Companies. the diffusion of water.Diffusion The simplest method of moving substances across the membrane is diffusion. oxygen molecules are always diffusing into the cell. like ethanol. a beaker is shown to demonstrate . either in the fluid within the cell or in your blood stream. there is always a higher oxygen concentration outside the cell and a lower concentration inside.4) and will occur across the plasma membrane as long as there is no restriction (e. diffusing into them until the cellular concentration is approximately equal to that in your bloodstream. For example. because oxygen is used for cellular respiration. the random movement of particles from an area of higher concentration to an area of lower concentration. Figure 3. Diffusion follows a concentration gradient (Figure 3. the sugar molecules continue to spread out in the water. also can diffuse freely through the plasma membrane. Permission granted for reproduction Osmosis Osmosis is the term for a special type of diffusion. Graphic showing the diffusion of a lump of sugar in four steps: Step 1.. 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. As oxygen follows this gradient from higher to lower concentration.g.4. 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. Non-polar lipids and small molecules such as oxygen and carbon dioxide are able to pass freely through the membrane. Inc. Steps 3 and 4. It affects these fairly rapidly and evenly. the sugar molecules beging to spread throughout the water.5). Other small molecules.

In the center frame. we take chemical bond energy and turn it into a form of energy that the cells can use. The first frame is isotonic. In the process of cellular respiration. These substances need some kind of carrier molecule to help them. will diffuse to the side with the lower water concentration (higher solute concentration).5. illustrated by the third frame. when you eat a potato. They must move through a protein that is imbedded in the plasma membrane. In step 1 a permeable membrane in a beaker of water causes water to distribute equally on either side of the membrane. you add a nondiffusible solute to the right side. which can cross the membrane. One of the molecules whose chemical bonds are broken down is glucose. as it goes through your digestion system. Water will move into your cells or out of your cells depending upon the concentration of solutes. In step 3. fluid replacement for an injured person must match the bloodstream's dissolved solute concentration. which will not cause water to leave or enter cells too rapidly. so water will flow from the left side of the beaker to the right. in your body tissues and in your blood stream. Inc. Water molecules. like salt. as is true of isotonic saline. For example. meaning the water molecules are evenly distributed between the two sides of the beaker. 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. until the water pressure is equal on both sides. there is less water pressure. the polymers of starch are broken down into . Although the movement of water is given a special name. which contains lots of starch. osmosis follows a concentration gradient (its own) and does not require the input of energy. Graphic depicting osmosis. Figure 3.the movement of water within a cell by osmosis. Permission granted for reproduction Facilitated Diffusion Many substances will follow a concentration gradient. Movment of Water by Osmosis ©The McGraw-Hill Companies. In step 2. diffusion causes the free water molecules on the non-solute side to move to the solute side. Therefore. but are too large to get through the membrane on their own. With the addition of these molecules.

See Figure 3.6. So this is an extremely important pump. In our nervous system. they're actually going against the concentration gradient. That is why it is called active transport. We call these proteins where this energy is used pumps because they are pumping substances against the concentration gradient. you have a concentration gradient.6 for an illustration of facilitated diffusion. There are carrier molecules in the cell membrane that are specific to glucose. 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. The same protein will move the molecule in either direction. one that has been well-studied is the sodium-potassium pump. Sodium and potassium are extremely important molecules. allowing my hand to move. sodium and potassium. the balance between these two ions. particularly in animals. and this type of movement across the plasma membrane does not require energy. This is part of the complexity of cell membranes. if I think that I am going to move my hand. When substances are going against their gradient. The concentration of glucose is usually higher outside a cell than it is inside. because you have to have different carrier molecules for different substances that are going to be brought into or excreted from the cell. because once it enters the cell it is broken down. In step 2. For instance. There are other carrier proteins for molecules such as amino acids. the protein helps or facilitates the movement of the molecule through the plasma membrane. substances are not going to go with the concentration gradient. In step 3. a molecule binds a particular protein that is embedded in the plasma membrane. It has been estimated . it is the gradient created by this pump that causes the message to be propagated down a nerve. but glucose is too big to move freely through the membrane. the molecule is released on the other side of the membrane. Proteins in the plasma membrane act as gates to allow movement of large molecules into and out of a cell.glucose monomers in your small intestine. Figure 3. then glucose is absorbed across the small intestine and goes into your blood stream. They do not allow other molecules through. Inc. The Movement of a Substance Through the Plasma Membrane Using a Carrier Molecule ©The McGraw-Hill Companies. That glucose is used by all of the cells in your body to provide energy. So. In step 1. allows the transmission of nerve impulses. energy must be used. There are many different pumps for different molecules. In this case.

the molecule is released on the other side of the membrane. allowing a number of different processes. there is a coupled channel protein that allows diffusion of sodium ions into the cell if it is coupled to glucose. This creates a concentration gradient with the higher concentration of sodium outside the cell. two potassium ions bind and are then transported to the inside of the cell. There are specific coupled channels for many needed molecules such as sugars and amino acids. Normally. it provides energy to change the shape of the protein channel. there is more sodium inside of a cell than outside. a molecule binds a particular protein that is embedded in the plasma membrane. as do ATP molecules which are the energy currency of the cells.7). Proteins in the plasma membrane act as gates to allow movement of large molecules into and out of a cell. 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. Sodium ions inside the cell attach to these proteins. and potassium inside the cell.that about 30 percent of the energy in our cells is used to maintain the concentration of sodium against its gradient. and this type of movement across the plasma membrane does not require energy. including transmission of nerve impulses and transport of nutrients into the cells. The same protein will move the molecule in either direction. allow .7. This concentration gradient is also used to help bring other substances into the cell against their concentration gradients. The Sodium-Potassium Pump ©The McGraw-Hill Companies. A transport protein in the membrane has specific receptors for sodium ions. it traps the sodium ions and they are pushed to the other side of the membrane (see Figure 3. For instance. Permission granted for reproduction On the outside of the membrane. When the ATP molecule splits. but there are many other ions that are pumped in and out of cells to establish concentration gradients for different reasons. facilitated diffusion. In step 2. These three methods. and active transport. Inc. In step 3. In step 1. It is important for the function of the protein channel to have this high sodium concentration outside of the cell. When the protein changes shape. through coupled channels (Figure 3. These pumps are important to maintaining cellular conditions. it "pulls" glucose along into the cell even though it is against the concentration gradient of the glucose. diffusion (including osmosis). So when the sodium ions diffused back into the cell. The sodium potassium pump is the most active. Figure 3.8). the protein helps or facilitates the movement of the molecule through the plasma membrane.

The membranes of the ER are continuous with the outer nuclear membrane. including the most primitive Giardia. or cannot.cells to regulate what can. these sodium ions can get back into the cell via the coupled channel as long as the pass through that channel with another molecule. These membranes are continuous. cross the plasma membrane. The sodiumpotassium pump creates a concentration gradient where there are more sodium ions outside of the cell. The endoplasmic reticulum (ER) is an organelle found in the cells of eukaryotic organisms. membrane-enclosed sacs or tube-like structures known as cisternae.[1] but is absent from red blood cells and spermatozoa. Endoplasmic reticulum occurs in most types of eukaryotic cells. such as sugar. The endoplasmic reticulum (ER) is a type of organelle in the eukaryotic cells that forms an interconnected network of flattened. There are two types of endoplasmic reticulum: rough and smooth. joining with the outer membrane of the nuclear membrane. It is an interconnected network of flattened sacs or tubes encased in membranes. Graphic depicts how the sodium-potassium channel is linked to another protein in the plasma membrane called a coupled channel. However. The rough endoplasmic reticulum is . The outer (cytosolic) face of the rough endoplasmic reticulum is studded with ribosomes that are the sites of protein synthesis.

the production of steroid hormones. and detoxification. The smooth endoplasmic reticulum lacks ribosomes and functions in lipid manufacture and metabolism. The phospholipid membrane encloses the cisternal space (or . 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.[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.especially prominent in cells such as hepatocytes. These sac-like structures are held together by the cytoskeleton.

depending on the changing metabolic activities of the cell. The functions of the endoplasmic reticulum can be summarized as the synthesis and export of proteins and membrane lipids. which is continuous with the perinuclear space but separate from the cytosol. Transformation can include embedding of new proteins in membrane as well as structural changes. The total animation time is about 2 minutes. The quantity of both rough and smooth endoplasmic reticulum in a cell can slowly interchange from one type to the other.lumen). 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 . but varies between ER and cell type and cell function. 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).

[4] The first 5-30 amino acids polymerized encode a signal peptide. 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. non-translating ribosomes are also known to stay associated with translocons. however.[5] The membrane of the rough endoplasmic reticulum forms large double membrane sheets . This special complex forms when a free ribosome begins translating the mRNA of a protein destined for the secretory pathway. which removes the signal peptide.[3] However. Ribosomes at this point may be released back into the cytosol. 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. a molecular message that is recognized and bound by a signal recognition particle (SRP). The binding site of the ribosome on the rough endoplasmic reticulum is the translocon. The protein is processed in the ER lumen by an enzyme (a signal peptidase)."rough" appearance (hence its name). A ribosome only binds to the RER once a specific proteinnucleic acid complex forms in the cytosol.

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

Oligosaccharyltransferase recognizes the AA sequence NXS or NXT (with the S/T residue phosphorylated) and adds a 14sugar backbone (2-N-acetylglucosamine. Smooth endoplasmic reticulum[edit] The smooth endoplasmic reticulum (abbreviated SER) has functions in several metabolic processes. It synthesizes lipids. Integral membrane proteins that stay embedded in the membrane as vesicles exit and bind to new membranes. This is N-linked (O-linking occurs in the Golgi). SNAP and SNARE proteins are key in the fusion event.secreted constitutively with no tag or secreted in a regulatory manner involving clathrin and paired basic amino acids in the signal peptide. and sebaceous glands have an abundance of smooth endoplasmic reticulum. Rab proteins are key in targeting the membrane. detoxification of natural metabolism products and of alcohol and drugs. . Cells which secrete these products. and 3-glucose at the end) to the side-chain nitrogen of Asn. and steroids. ovaries. N-linked glycosylation: If the protein is properly folded. phospholipids. such as those in the testes. 9branching mannose. Initial glycosylation as assembly continues. [10] It also carries out the metabolism of carbohydrates.

These tubes sometimes branch forming a network that is reticular in appearance. it regulates calcium ion concentration. The smooth endoplasmic reticulum also contains the enzyme glucose-6-phosphatase. there are dilated areas like the sacs of rough endoplasmic reticulum. The sarcoplasmic reticulum (SR). and it serves different functions in each. 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. It is connected to the nuclear envelope and consists of tubules that are located near the cell periphery. Smooth endoplasmic reticulum is found in a variety of cell types (both animal and plant). from the Greek σάρξ sarx ("flesh").[11] In muscle cells. and steroid metabolism.[6] In some cells. The only structural difference . a step in gluconeogenesis. is smooth ER found in myocytes.attachment of receptors on cell membrane proteins. with sarcoplasmic reticulum colored in blue. which converts glucose-6-phosphate to glucose. Sarcoplasmic reticulum[edit] Skeletal muscle fiber.

[14] Functions[edit] The endoplasmic reticulum serves many general functions. including protein disulfide isomerase (PDI).between this organelle and the smooth endoplasmic reticulum is the medley of proteins they have. Correct folding of newly made proteins is made possible by several endoplasmic reticulum chaperone proteins.[12][13] After their release from the sarcoplasmic reticulum. calreticulin. calcium ions interact with contractile proteins that utilize ATP to shorten the muscle fiber. This fundamental difference is indicative of their functions: The endoplasmic reticulum synthesizes molecules. including the folding of protein molecules in sacs called cisternae and the transport of synthesized proteins in vesicles to the Golgi apparatus. Only properly folded proteins are transported from the rough . calnexin. the Hsp70 family member BiP/Grp78. and the peptidylpropyl isomerase family. ERp29. both bound to their membranes and drifting within the confines of their lumens. while the sarcoplasmic reticulum stores calcium ions and pumps them out into the sarcoplasm when the muscle fiber is stimulated. The sarcoplasmic reticulum plays a major role in excitation-contraction coupling.

[17] The fluid mosaic model explains various observations regarding the structure of functional cell membranes. Disturbances in redox regulation. calcium regulation. glucose deprivation. This stress is emerging as a potential cause of damage in hypoxia/ischemia.ER to the Golgi apparatus – unfolded proteins cause an unfolded protein response as a stress response in the ER. 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. insulin resistance. a state in which the folding of proteins slows. Another way to define membrane domains is the association of the lipid membrane with the cytoskeleton . describes the cell membrane as a two-dimensional liquid in which that restrict the lateral diffusion of membrane components. leading to an increase in unfolded proteins. and viral infection[15] or the overexpression of proteins[16] can lead to endoplasmic reticulum stress response (ER stress). The model. and other disorders. which was devised by SJ Singer and GL Nicolson in 1972.

In vertebrates. receptor-mediated endocytosis. A microbody is a type of organelle that is found in the cells of plants. macropinocytosis. caveolae. and cell fusion. and phagocytosis. glycosomes and hydrogenosomes. Organelles in the microbody family include peroxisomes. including: cell-cell signaling.filaments and the extracellular matrix through membrane proteins. cell division. apoptosis.[1] The current model describes important features relevant to many cellular processes. Schematic drawing illustrating clathrin-mediated (left) and clathrin-independent endocytosis (right) of synaptic vesicle membranes. microbodies are especially prevalent in the liver and kidney organs. protozoa.[1] . Endocytosis pathways can be subdivided into four categories: namely. membrane budding. and animals. glyoxysomes.

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.g. antibodies and many others. growth factors. Coated pits can concentrate large extracellular molecules that have different receptors responsible for the receptormediated endocytosis of ligands.Clathrin-mediated endocytosis is mediated by small (approx.[2] . e. Clathrin-coated vesicles (CCVs) are found in virtually all cells and form domains of the plasma membrane termed clathrin-coated pits. transferrin. low density lipoprotein.

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