320Fall09Homework6 - normal levels of enzymes. Assuming...

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Cell Biology (BIO 320), Fall 2009, Dr. Bushart Homework set #6 1. What are two factors that might prevent vesicles that undergo homotypic fusion from simply fusing back with their parent membrane? 2. What will happen to protein “X” in the ER if it contains no specific retention signals and is not recognized by any particular transport receptor proteins (i.e. what is the default pathway for proteins entering the ER)? How does this compare to the BiP chaperone? 3. There are a number of lysosomal diseases. One particular form, called I-cell disease, stems from the inability of the cells to correctly tag their enzymes with M6P. a. Where will these enzymes lacking M6P tags end up? Why? b. Certain cells in animals with I-cell disease still have lysosomes with near-
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Unformatted text preview: normal levels of enzymes. Assuming these cells have no unique pathway (i.e. think about pathways you know!) for directed delivery of lysosomal enzymes, how would you trace their arrival to the lysosome? 4. What are two ways that the ER is protected from the actions of the acid hydrolases it transports forward to the Golgi? 5. How is the functionality and activity of KDEL receptors similar to that of M6P receptors? How are they different? 6. Specifically, why would protein processing now work correctly for a protein progressing through the Golgi in the trans to cis direction, even if the protein eventually passes through all of the cisternae?...
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This note was uploaded on 01/25/2010 for the course BIO 51055 taught by Professor Bushart during the Fall '09 term at University of Texas at Austin.

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