Structural highlights
Function
[EXOC6_DROME] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding.
Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo.,Wu S, Mehta SQ, Pichaud F, Bellen HJ, Quiocho FA Nat Struct Mol Biol. 2005 Oct;12(10):879-85. Epub 2005 Sep 11. PMID:16155582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu S, Mehta SQ, Pichaud F, Bellen HJ, Quiocho FA. Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat Struct Mol Biol. 2005 Oct;12(10):879-85. Epub 2005 Sep 11. PMID:16155582 doi:10.1038/nsmb987
