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14 Cards in this Set
- Front
- Back
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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. |
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What enzyme allows for disulfide bonds to form? |
Disulfide isomerase |
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Why are there few disulfide bonds in the cytoplasm? |
It's a reducing environment, so it's SH instead of S-S |
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What happens to proteins that are incorrectly folded? |
a. retrotranslocation out of the er b. ubiquination c. proteostome destroys |
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what enzyme performs glyocolysation of new proteins? when does it happen? |
oligosaccharyl transferase during translation |
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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 |
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what happens in cis golgi network? |
phosphorylation of oligosaccharides on lysosomal proteins |
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what happens in trans golgi |
sorting |
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what was the evidence for the cisternal maturation theory? |
the yeast experiment showed the cis turning to trans color (green > red) |
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how do lysosomes have an acidic pH? |
they have a proton pump |
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what are the 3 ways lysosomes receive material? |
1. phagocytosis 2. endocytosis 3. autophagy |
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how do lysosomal proteins get targeted from the ER? |
M6P; phosphate put on mannose in cis golgi |
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how is it decided which proteins get the lysosomal m6p? |
lysosomal signal patch |
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