Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
- 11 September 2005
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Structural & Molecular Biology
- Vol. 12 (10), 879-885
- https://doi.org/10.1038/nsmb987
Abstract
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-Å crystal structure of the C-terminal domain revealed a novel fold consisting of ten α-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.Keywords
This publication has 45 references indexed in Scilit:
- Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cellsJournal of Cell Science, 2004
- The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulinNature, 2003
- Mutations in the Exocyst Component Sec5 Disrupt Neuronal Membrane Traffic, but Neurotransmitter Release PersistsNeuron, 2003
- The Exocyst Complex Associates with Microtubules to Mediate Vesicle Targeting and Neurite OutgrowthJournal of Neuroscience, 2001
- The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosisThe EMBO Journal, 1999
- Sec6/8 Complex Is Recruited to Cell–Cell Contacts and Specifies Transport Vesicle Delivery to the Basal-Lateral Membrane in Epithelial CellsCell, 1998
- Sec3p Is a Spatial Landmark for Polarized Secretion in Budding YeastCell, 1998
- Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae.The Journal of cell biology, 1995
- The molecular machinery for secretion is conserved from yeast to neurons.Proceedings of the National Academy of Sciences of the United States of America, 1993
- Identification of 23 complementation groups required for post-translational events in the yeast secretory pathwayCell, 1980