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14 Cards in this Set

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What happens with protein folding in ER? What happens if it's not folded correctly?

1. Correct folding requires "chaperones" - BIP


2. If folded incorrectly it stays in the protein (eg cystic fibrosis mutant gene)


3.

What enzyme allows for disulfide bonds to form?

Disulfide isomerase



Why are there few disulfide bonds in the cytoplasm?

It's a reducing environment, so it's SH instead of S-S

What happens to proteins that are incorrectly folded?

a. retrotranslocation out of the er


b. ubiquination


c. proteostome destroys

what enzyme performs glyocolysation of new proteins? when does it happen?

oligosaccharyl transferase


during translation

Why are oligosaccharides added?

1. helps protein assume correct formation


2. makes protein more water soluble


3. makes the protein more resistant to proteases


4. helps target lysosomal proteins to lysosome


5. serves in quality control

what happens in cis golgi network?

phosphorylation of oligosaccharides on lysosomal proteins

what happens in trans golgi

sorting

what was the evidence for the cisternal maturation theory?

the yeast experiment showed the cis turning to trans color (green > red)

how do lysosomes have an acidic pH?

they have a proton pump

what are the 3 ways lysosomes receive material?

1. phagocytosis


2. endocytosis


3. autophagy

how do lysosomal proteins get targeted from the ER?

M6P; phosphate put on mannose in cis golgi

how is it decided which proteins get the lysosomal m6p?

lysosomal signal patch