Exocyst
The exocyst is an octameric protein complex involved in vesicle trafficking, specifically the tethering and spatial targeting of post-Golgi vesicles to the plasma membrane prior to vesicle fusion. It is implicated in a number of cell processes, including exocytosis, cell migration, and growth.
Subunits[edit]
The exocyst is composed of eight subunits, whose nomenclature differs between mammalian cells and Saccharomyces cerevisiae.
| Subunit | Mammalian cells | Saccharomyces cerevisiae |
|---|---|---|
| 1 | EXOC1 | Sec3 |
| 2 | EXOC2 | Sec5 |
| 3 | EXOC3 | Sec6 |
| 4 | EXOC4 | Sec8 |
| 5 | EXOC5 | Sec10 |
| 6 | EXOC6 | Sec15 |
| 7 | EXOC7 | Exo70 |
| 8 | EXOC8 | Exo84 |
Function[edit]
The exocyst complex serves to direct vesicles after the Golgi complex to specific locations on the plasma membrane and to mediate their tethering and localization to the membrane immediately before fusion. The exocyst complex has also been implicated in the active trafficking of mitochondria from immune cells to cancer cells. [1] Because of this function, the exocyst complex is heavily involved in exocytosis. Sec3 (EXOC1) and Exo70 (EXOC7) are localized to the plasma membrane, and are physically attached to the membrane by Rho GTPases such as CDC42. Other complementary exocyst components such as Sec15 (EXOC6) and Sec4 are localized to the vesicle membrane. Exocyst proteins on the plasma membrane bind vesicular exocyst proteins, bringing the vesicle very close to the plasma membrane in a fashion similar to the SNARE interactions to facilitate fusion.
The exocyst also interacts with Rho GTPases responsible for controlling cell polarity and the activity of the cytoskeleton.
History[edit]
Hints of a multi-subunit complex involved in yeast exocytosis came from work in Peter Novick's group, then at Yale University School of Medicine, in the early 1990s.[2] Works led by Robert Bowser and Daniel TerBush in 1992 and 1995 respectively isolated Sec6p and Sec8p, showing them to participate in a complex of at least eight proteins, found at the site of active exocytosis.[2][3][4] In 1996, the same group identified the exocyst member proteins in yeast and coined the name "exocyst" for the complex.[2][5]
References[edit]
- ^ Saha T, Dash C, Jayabalan R, et al. (2021). "Intercellular nanotubes mediate mitochondrial trafficking between cancer and immune cells". Nat. Nanotechnol. doi:10.1038/s41565-021-01000-4. PMC 10071558.
- ^ a b c Hsu SC, TerBush D, Abraham M, Guo W (2004). "The exocyst complex in polarized exocytosis". Int Rev Cytol. 233: 243–65. doi:10.1016/S0074-7696(04)33006-8. PMID 15037366.
- ^ Bowser R, Müller H, Govindan B, Novick P (September 1992). "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. 118 (5): 1041–56. doi:10.1083/jcb.118.5.1041. PMC 2289594. PMID 1512289.
- ^ TerBush DR, Novick P (July 1995). "Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae". J Cell Biol. 130 (2): 299–312. doi:10.1083/jcb.130.2.299. PMC 2199927. PMID 7615633.
- ^ TerBush DR, Maurice T, Roth D, Novick P (December 1996). "The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae". EMBO J. 15 (23): 6483–94. PMC 452473. PMID 8978675.
External links[edit]
- https://web.archive.org/web/20051224051252/http://www.umassmed.edu/faculty/graphics/208/munson-figure-1.jpg
- http://www.jbc.org/cgi/content/full/279/41/43027 Archived 2005-11-25 at the Wayback Machine
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