ER Flashcards

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1
Q

where are most proteins begin synthesis?

A

on ribisomes in the cytosol

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2
Q

where (and how) do new proteins go?

A

to the organelle where it functions, by sorting signals in amino acid sequence

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3
Q

what are the main steps of the secretory pathway?

A

1 - translates from mRNA in ribisomes to cytoplasm
2 - enters ER lumen
3 - goes from the Er to the golgi in a vesicle
4 - transits the golgi
5 - exits golgi in vesicle
6 - vesicle fuses cell membrane
7 - its outside!!!!!!

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4
Q

what are the types of mutants?

A

1 - fail ER import
2 - fail to produce ER vesicles
3 - vesicles dont fuse to golgi
4 - fail to leave golgi (golgi vesicles dont form)
5 - vesicles dont fuse with cell membrane

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5
Q

where were the main proteins in protein trafficking discovered?

A

in yeast

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6
Q

how is the ER organized?

A

into a netlike labyrinth of branching tubules and flattened sacs that extend throughout the cytosol

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7
Q

what is the difference between the rough and smooth ER?

A

rough has ribisomes bound to membrane surface, smooth doesn’t and is used in biosynthesis and metabolism of lipids

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8
Q

what is cotranslational import into the ER?

A

the first step in protein secretion

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9
Q

how is the ER signal sequence guided to the ER membrane?

A

signal reception particle (SRP) that binds to a signal sequence
SRP receptor in ER membrane

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10
Q

what happens when signal sequence binds?

A

SRP exposes a binding site for SRP receptor (transmembrane protein complex in the rough ER membrane)

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11
Q

what do membrane-bound ER ribisomes do?

A

make proteins that are co-translocated across the ER membrane

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12
Q

what is a translocator (or translocon)?

A

has a signal sequence gated aqueous channel that polypeptide chain passes throgh

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13
Q

where to translocated polypeptide chains fold and assemble?

A

in the rough ER lumen

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14
Q

what are disulfide bonds?

A

post-translational modifications (occur in the ER)
part of tertiary structure

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15
Q

what are oligosaccharides used for?

A

as tags to mark the state of protein folding (folded properly - remove last glucose, folded improperly - add a glucose)

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15
Q

what forms disulfide bonds?

A

protein disulfide-isomerase (PDI)

15
Q

what happens to proteins synthesized in the rough ER?

A

they are glycosylated by the addition of a common N-linked oligosaccharide

16
Q

what does calnexin do?

A

binds to monoglycosylated (on completely folded proteins) and keeps them in the ER

17
Q

what is calnexin?

A

a chaperone that recruits oxidoreductase to add more disulphide bonds

18
Q

what do ER chaperones do?

A

prevent protein misfolding and aggregation (protects peptides from ineracting with misfolded proteins and creates a folding environment to give it a second chance), can also unfold them to let them fold properly

18
Q

how are misfolded proteins recognized?

A

they have exposed hydrophobic residues (shouldn’t be outside) that are recognized by folding sensors

18
Q

what are two examples of Er chapersones?

A

Hsp70 and BiP