MGD Session 6 INCOMPLETE Flashcards

1
Q

What is meant by constitutive secretion?

A

It is a continuous process of protein regulation. The proteins are packaged into vesicles and are continually released by exocytosis.

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2
Q

Give 2 proteins secreted by constitutive secretion.

A

Serum albumin, collagen

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3
Q

What is regulated secretion?

A

Proteins are released in response to a signal. They are packaged into vesicles but not released until the stimulus is received.

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4
Q

Give an example of a protein secreted by regulated secretion.

A

Insulin

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5
Q

Explain the first 5 steps of the protein secretion pathway.

A
  1. Free ribosome initiates protein synthesis from mRNA molecule
  2. Hydrophobic N-terminal signal sequence is produced.
  3. Signal recognition particle recognises newly formed protein & synthesis stops.
  4. SRP (GTP-bound) directs the ribosome to the SRP receptors on the cytosolic face of the ER.
  5. SRP dissociates
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6
Q

Explain what happens after the SRP dissociates in the protein secretion pathway.

A
  1. Protein synthesis continues and feeds the new polypeptide into the ER via a pore in the membrane (peptide translocation complex)
  2. Signal sequence is removed by a signal peptidase
  3. Ribosome dissociates and is recycled.
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7
Q

What are the 4 things required for protein sorting?

A

A signal intrinsic to the protein
A receptor that recognises the signal and directs it to the correct membrane
A translocation machinery
Energy to transfer the protein to its new place

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8
Q

Where do you find the signal sequence on a protein?

A

At the N-terminus.

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9
Q

Name 3 kinds of cells where regulated secretion takes place

A

Endocrine cells
Exocrine cells
Neurocrine cells

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10
Q

What is SRP?

A

Signal Recognition Particle.
It is a multidomain riboprotein that mediates 3-way association with the SRP receptor in the ER, the ribosome and the signal peptide.

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11
Q

What protein modifications can take place in the ER? (name 3 and the enzymes that they require)

A
Signal cleavage (signal peptidase)
Disulphide bond formation (protein disulphide isomerase)
N-linked glycosylation (oligosaccharide-protein transferase)
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12
Q

What protein modifications can take places in the golgi apparatus? Name 3

A

O-linked glycosylation by glycosyl transferase
Trimming and modification of N-linked oligosaccharides
Proteolytic processing

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13
Q

What is N-linked glycosylation?

A

A carbohydrate is added via N-glycosyl link to the nitrogen of the amide group of an asparagine amino acid from a Dolichol phosphate carrier molecule.

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14
Q

What is Dolichol phosphate?

A

A long chain hydrocarbon molecule that inserts into the membrane of the ER with its phosphate group protruding.and an oligosaccharide attached.

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15
Q

Where does O-linked glycosylation take place?

A

Golgi apparatus

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16
Q

What is O-linked glycosylation?

A

Carbohydrate is added via a glycosidic link to the hydroxyl group on Serine or Threonine. Glycosyl transferase builds up a sugar chain from Nucleotide sugar substrates.