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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Grote, E. Carr, C. M. Novick, P. J. |
| Description | Author Affiliation: Grote E ( Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.) |
| Abstract | In yeast, assembly of exocytic soluble N-ethylmaleimide–sensitive fusion protein (NSF) attachment protein receptor (SNARE) complexes between the secretory vesicle SNARE Sncp and the plasma membrane SNAREs Ssop and Sec9p occurs at a late stage of the exocytic reaction. Mutations that block either secretory vesicle delivery or tethering prevent SNARE complex assembly and the localization of Sec1p, a SNARE complex binding protein, to sites of secretion. By contrast, wild-type levels of SNARE complexes persist in the sec1-1 mutant after a secretory block is imposed, suggesting a role for Sec1p after SNARE complex assembly. In the sec18-1 mutant, cis-SNARE complexes containing surface-accessible Sncp accumulate in the plasma membrane. Thus, one function of Sec18p is to disassemble SNARE complexes on the postfusion membrane. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 2 |
| Volume Number | 151 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2000-10-16 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Exocytosis Fungal Proteins Metabolism Membrane Fusion Membrane Proteins Saccharomyces Cerevisiae Proteins Vesicular Transport Proteins Carrier Proteins Cell Membrane Cell Polarity GTP-Binding Proteins Guanine Nucleotide Exchange Factors Models, Biological Munc18 Proteins N-Ethylmaleimide-Sensitive Proteins Nerve Tissue Proteins Qa-SNARE Proteins R-SNARE Proteins SNARE Proteins Transport Vesicles Yeasts Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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