Lecture 7, retrieval to ER with movie

Lecture 7, retrieval to ER with movie - Lecture 7 Resident...

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Lecture 7 Resident ER proteins
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What happens to polypeptides that are transported into the ER? 1. Many become N-linked glycosylated and undergo glucose trimming and addition. 2. Disulfide bond formation on some. 3. Protein folding for all, and export of misfolded proteins back into cytosol (so called quality control of protein folding).
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Traffic between ER and Golgi occurs in both directions! Page 766 Molecular Biology of the Cell (© Garland Science 2008)
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COPII coated vesicles: ER --> cis-Golgi COPI coated vesicles: cis-Golgi --> ER COPII: anterograde transport COPI: retrograde (retrieval) transport Figure 13-23b Molecular Biology of the Cell (© Garland Science 2008)
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Why do cells need retrograde transport (Golgi --> ER)?????
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Bip is a soluble molecular chaperone (i.e., not membrane-bound) that helps proteins fold in the ER lumen. Since it functions in the ER lumen, it must reside there. PDI is another example of a soluble ER resident protein. How are such proteins retained in the ER in the face of enormous flux from ER?
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proteins remain in the ER? 1. Hypothesis: Signal sequence on soluble resident ER proteins either acts to retain proteins in the ER or acts to retrieve such proteins from a later secretory compartment back to the ER. 2. How would you identify this signal sequence?
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This note was uploaded on 09/19/2011 for the course BIO 320 taught by Professor Staff during the Spring '08 term at University of Texas at Austin.

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Lecture 7, retrieval to ER with movie - Lecture 7 Resident...

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