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Dissertation
Sphingolipid-dependent endocytosis of multiple sugar transporters
Doctor of Philosophy (Ph.D.), Drexel University
Aug 2006
DOI:
https://doi.org/10.17918/00010281
Abstract
Rvs161 is a homologue of the mammalian amphiphysin protein, which has been shown to be involved in endocytosis at synaptic vesicles. Yeast cells lacking Rvs161 have pleiotrophic defects, including endocytosis defects. SUR4 encodes a very long chain fatty acid elongase that is involved in the sphingolipid biosynthetic pathway. Loss of function of SUR4 alters the composition of sphingolipids produced in the yeast cell; in particular, long chain sphingoid bases accumulate in sur4 cells. Loss of function of SUR4 in rvs161 cells re-initiates endocytosis. We are using rvs161 sur4 cells as a model to explore sphingolipid-dependent endocytosis. Studies have identified a long chain base (LCB) dependent endocytic pathway and the cell factors required for its function. rvs161 cells properly localize multiple sugar transporter protein(s) but are unable to endocytose these transporters. Rvs161 is required for endocytosis of these transporters: rvs161 cells accumulate these transporters at the plasma membrane under conditions when these transporters would normally undergo endocytosis and degradation. Deletion of SUR4 re-initiates sugar transporter endocytosis in rvs161 cells. We found that re-initiation of transporter endocytosis requires DOA1, DOA4 and RSP5. Using the endocytosis of the high affinity glucose transporter Hxt2-GFP, we have found a requirement for ceramide activated protein phosphatases (CAPP), the B subunit of which is Cdc55, in long chain base dependent endocytosis.
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Details
- Title
- Sphingolipid-dependent endocytosis of multiple sugar transporters
- Creators
- Jeanelle Marie Morgan
- Contributors
- Joseph T. Nickels (Advisor) - Drexel University, Drexel University (1970-)
- Awarding Institution
- Drexel University
- Degree Awarded
- Doctor of Philosophy (Ph.D.)
- Publisher
- Drexel University; Philadelphia, Pennsylvania
- Number of pages
- xiv, 141 pages
- Resource Type
- Dissertation
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; College of Medicine; Drexel University
- Other Identifier
- 991021888969004721