| Structural highlights
Function
[SEC15_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.[1] [SEC6_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. [EXO70_YEAST] Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in the assembly of the exocyst.[2] [SEC5_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. [EXO84_YEAST] Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis and to the budding site. Also involved in assembly of the spliceosome.[3] [4] [5] [SEC3_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. [SEC8_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. [SEC10_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Publication Abstract from PubMed
The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the structure of the Saccharomyces cerevisiae exocyst complex at an average resolution of 4.4 A. Our model revealed the architecture of the exocyst and led to the identification of the helical bundles that mediate the assembly of the complex at its core. Sequence analysis suggests that these regions are evolutionarily conserved across eukaryotic systems. Additional cell biological data suggest a mechanism for exocyst assembly that leads to vesicle tethering at the plasma membrane.
Cryo-EM structure of the exocyst complex.,Mei K, Li Y, Wang S, Shao G, Wang J, Ding Y, Luo G, Yue P, Liu JJ, Wang X, Dong MQ, Wang HW, Guo W Nat Struct Mol Biol. 2018 Jan 15. pii: 10.1038/s41594-017-0016-2. doi:, 10.1038/s41594-017-0016-2. PMID:29335562[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bowser R, Muller H, Govindan B, Novick P. Sec8p and Sec15p are components of a plasma membrane-associated 19.5S particle that may function downstream of Sec4p to control exocytosis. J Cell Biol. 1992 Sep;118(5):1041-56. PMID:1512289
- ↑ Wiederkehr A, De Craene JO, Ferro-Novick S, Novick P. Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p. J Cell Biol. 2004 Dec 6;167(5):875-87. PMID:15583030 doi:http://dx.doi.org/jcb.200408001
- ↑ Guo W, Grant A, Novick P. Exo84p is an exocyst protein essential for secretion. J Biol Chem. 1999 Aug 13;274(33):23558-64. PMID:10438536
- ↑ Awasthi S, Palmer R, Castro M, Mobarak CD, Ruby SW. New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA splicing. J Biol Chem. 2001 Aug 17;276(33):31004-15. Epub 2001 Jun 25. PMID:11425851 doi:http://dx.doi.org/10.1074/jbc.M100022200
- ↑ Zhang X, Zajac A, Zhang J, Wang P, Li M, Murray J, TerBush D, Guo W. The critical role of Exo84p in the organization and polarized localization of the exocyst complex. J Biol Chem. 2005 May 27;280(21):20356-64. Epub 2005 Mar 23. PMID:15788396 doi:http://dx.doi.org/M500511200
- ↑ Mei K, Li Y, Wang S, Shao G, Wang J, Ding Y, Luo G, Yue P, Liu JJ, Wang X, Dong MQ, Wang HW, Guo W. Cryo-EM structure of the exocyst complex. Nat Struct Mol Biol. 2018 Jan 15. pii: 10.1038/s41594-017-0016-2. doi:, 10.1038/s41594-017-0016-2. PMID:29335562 doi:http://dx.doi.org/10.1038/s41594-017-0016-2
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