B: ER, Trafficking, Co-translational Import (19) Flashcards

1
Q

What is the ER

A

Endoplasmic reticulum

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2
Q

What is the structure of the ER

A

Mosaic structure with many cell types inside

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3
Q

What is found in the rough ER

A

Associated with ribosomes
Many proteins, including those destined for secretion are synthesized by ribosomes associated with the rough ER

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4
Q

What is found in the smooth ER

A

Lacks ribosomes
Primary site of lipid synthesis

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5
Q

Does the RER or SER have ribosomes

A

Rough ER

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5
Q

What are the functions of the smooth ER (4)

A
  1. Lipid synthesis
  2. Production steroid hormones
  3. Detoxification
  4. Sequestration
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6
Q

What steroid hormones are produced in the SER

A

Ex. glucocorticoids, androgens and estrogens - endocrine cells

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7
Q

How does detoxification occur in the SER

A

Liver cells contain enzymes that modify foreign compounds

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8
Q

What sequestration occurrs in the SER

A

Storage of Ca

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9
Q

Why does the cell need to put energy into controlling Calcium levels

A

Ca2+ does not bind water very well, which will precipitate phosphates and make proteins insoluble

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10
Q

How does the cell control Ca levels

A

Calcium in the cytosol is either bond by a range of Ca2+ binding proteins, forced out through pumps and transporters or sequestered into specific organelles

Often referred to as Ca2+ sinks or pools

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11
Q

What are the 4 functions of the rough ER

A
  1. Synthesis of membrane phospholipids
  2. Glycosylation of proteins
  3. Protein folding - quality control
  4. Protein synthesis, modification and transport
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12
Q

Explain protein folding within the RER

A

Involve activity of molecular chaperones, specific types of protein that assist in folding process

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13
Q

Where are proteins targeted to in the RER (3)

A

Proteins targeted to ER

Proteins targeted to other endomembrane compartments (soluble and transmembrane)

Proteins targeted to plasma membrane (secreted and transmembrane)

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14
Q

What do ribosomes synthesize in the cytoplasm?

A

In the cytoplasm, ribosomes synthesize polypeptides from mRNA

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15
Q

What are the 4 components of protein synthesis

A
  1. Searching for start codon
  2. Beginning of elongation
  3. Elongation
  4. Termination
16
Q

Explain the first step of protein synthesis:
Searching for start codon

A

Initiation factors recruit the small ribosomal subunit and tRNA and scan the mRNA for a start codon

17
Q

Explain the second step of protein synthesis: Beginning of elongation

A

Once the complex reaches AUG, the large ribosomal subunit joins

The initiation factor is released

A tRNA complementary to the next codon binds to the A site

18
Q

Explain the third step of protein synthesis:
Elongation

A

A reaction transfers the Met to the AA on the tRNA in the A site, forming a peptide bond

The ribosome moves down 1 codon, which puts the AA carrying the polypeptide into the P site and the now-uncharged tRNA into the E site where it is ejected

A new tRNA complementary to the next codon binds to the A site

19
Q

What are free ribosomes

A

Ribosomes not associated with the ER

20
Q

Where does all protein translation begin

A

All protein translation begins on free ribosomes

21
Q

Where is protein translation completed

A

Translation is completed with free or ER bound ribosomes

22
Q

What type of proteins are translated with free ribosomes

A

Cytosolic proteins

Peripheral membrane proteins

Proteins targeted to nucleus, mitochondria, peroxisomes, chloroplasts

23
Q

What type of proteins are translated with ER bound ribosomes

A

Secreted proteins

Integral membrane proteins

Soluble proteins associated with inside (lumen) of endomembrane system

24
Q

What is a signal sequence

A

Signal sequence is:

  • Located in amino-terminus (N-terminus)
  • Contains several consecutive hydrophobic AAs
  • Directs synthesis to the ER compartment
25
Q

What does a signal sequence do

A

Moves ribosomes to the ER to target protien

26
Q

What happens to ribosomes once they are in the ER

A

Ribosomes form protein

Protein moves through channel into ER for cotranslational import

27
Q

What is cotranslational protein import

A

The transport of a polypeptide chain occurs while it is being synthesized on a ribosome bound to the channel

28
Q

What are the 4 steps of cotranslational protein import

A
  1. After translation of signal sequence, a signal recognition particle (SRP) binds to signal sequence and stops the translation process
  2. SRP binds to SRP receptor to target the whole translation complex to ER
  3. SRP is released and the ribosome binds to translocon. Once this is done, protein synthesis resumes
  4. Polypeptide enters the ER (through the translocon) as it is translated. In the end, the signal peptide is cleaved off and the chaperone folds the protein
29
Q

How are proteins targeted to the mitochondria

A

For mitochondria, the TOM complex is the equivalent of SRP complex and translocon

30
Q

What are the 2 endocytic pathways of protein sorting

A
  1. It is retained in the ER lumen, if that is where it functions
  2. It is transported from the ER to the golgi complex for further meditation and delivered to distal paths of biosynthetic/secretory pathways.