Structural highlights
Function
SEC17_YEAST SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs, which are required for interactions in trans during docking and fusion steps. Can displace HOPS from SNARE complexes, which may be a prerequisite for trans-SNARE complex disassembly and subsequent rounds of priming, docking and fusion.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Mayer A, Wickner W, Haas A. Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell. 1996 Apr 5;85(1):83-94. PMID:8620540
- ↑ Haas A, Wickner W. Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF). EMBO J. 1996 Jul 1;15(13):3296-305. PMID:8670830
- ↑ Nichols BJ, Ungermann C, Pelham HR, Wickner WT, Haas A. Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature. 1997 May 8;387(6629):199-202. PMID:9144293 doi:http://dx.doi.org/10.1038/387199a0
- ↑ Collins KM, Thorngren NL, Fratti RA, Wickner WT. Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J. 2005 May 18;24(10):1775-86. Epub 2005 May 5. PMID:15889152 doi:http://dx.doi.org/7600658
