The Exocyst Complex in Polarized Exocytosis

Overview

Journal Curr Opin Cell Biol

Publisher Elsevier

Specialty Cell Biology

Date 2009 May 29

PMID 19473826

Citations 213

Authors

Bing He

Wei Guo

Affiliations

Soon will be listed here.

Abstract

The exocyst is an octameric protein complex, which mediates the tethering of post-Golgi secretory vesicles to the plasma membrane before exocytic fusion. The exocyst assembles by side-by-side packing of rod-shaped subunits composed of helical bundles. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the exocyst with PI(4,5)P(2). In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex. Here we review the recent advances in the field, focusing on the function of the exocyst in polarized exocytosis.

Citing Articles

The Exocyst Subunits EqSec5 and EqSec6 Promote Powdery Mildew Fungus Growth and Pathogenicity.

Yin J, Zhu X, Chen Y, Lv Y, Shan J, Liu Y J Fungi (Basel). 2025; 11(1).

PMID: 39852492 PMC: 11767214. DOI: 10.3390/jof11010073.

Molecular mechanisms of mTOR-mediated cisplatin response in tumor cells.

Maharati A, Rajabloo Y, Moghbeli M Heliyon. 2025; 11(1):e41483.

PMID: 39834411 PMC: 11743095. DOI: 10.1016/j.heliyon.2024.e41483.

Emerging Roles of Exocyst Complex in Fungi: A Review.

Zuriegat Q, Abubakar Y, Wang Z, Chen M, Zhang J J Fungi (Basel). 2024; 10(9).

PMID: 39330374 PMC: 11433146. DOI: 10.3390/jof10090614.

Roles for the canonical polarity machinery in the establishment of polarity in budding yeast spores.

Cooperman B, McMurray M bioRxiv. 2024; .

PMID: 39257763 PMC: 11383998. DOI: 10.1101/2024.08.29.610423.

Systematic review and meta-analysis of genome-wide pooled CRISPR screens to identify host factors involved in influenza A virus infection.

Maes A, Botzki A, Mathys J, Impens F, Saelens X J Virol. 2024; 98(5):e0185723.

PMID: 38567969 PMC: 11257101. DOI: 10.1128/jvi.01857-23.

References

Grosshans B, Andreeva A, Gangar A, Niessen S, Yates 3rd J, Brennwald P . The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p. J Cell Biol. 2006; 172(1):55-66. PMC: 2063532. DOI: 10.1083/jcb.200510016. View

Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rosse C . ARF6 controls post-endocytic recycling through its downstream exocyst complex effector. J Cell Biol. 2003; 163(5):1111-21. PMC: 2173613. DOI: 10.1083/jcb.200305029. View

Sivaram M, Saporita J, Furgason M, Boettcher A, Munson M . Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p. Biochemistry. 2005; 44(16):6302-11. DOI: 10.1021/bi048008z. View

Bao Y, Lopez J, James D, Hunziker W . Snapin interacts with the Exo70 subunit of the exocyst and modulates GLUT4 trafficking. J Biol Chem. 2007; 283(1):324-331. DOI: 10.1074/jbc.M706873200. View

Dong G, Hutagalung A, Fu C, Novick P, Reinisch K . The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol. 2005; 12(12):1094-100. DOI: 10.1038/nsmb1017. View

Roumanie O, Wu H, Molk J, Rossi G, Bloom K, Brennwald P . Rho GTPase regulation of exocytosis in yeast is independent of GTP hydrolysis and polarization of the exocyst complex. J Cell Biol. 2005; 170(4):583-94. PMC: 2171504. DOI: 10.1083/jcb.200504108. View

Adamo J, Rossi G, Brennwald P . The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. Mol Biol Cell. 1999; 10(12):4121-33. PMC: 25747. DOI: 10.1091/mbc.10.12.4121. View

Grindstaff K, Yeaman C, Anandasabapathy N, Hsu S, Rodriguez-Boulan E, Scheller R . Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell. 1998; 93(5):731-40. DOI: 10.1016/s0092-8674(00)81435-x. View

Robinson N, Guo L, Imai J, Toh-E A, Matsui Y, Tamanoi F . Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol Cell Biol. 1999; 19(5):3580-7. PMC: 84150. DOI: 10.1128/MCB.19.5.3580. View

10.

Munson M, Novick P . The exocyst defrocked, a framework of rods revealed. Nat Struct Mol Biol. 2006; 13(7):577-81. DOI: 10.1038/nsmb1097. View

11.

Whyte J, Munro S . The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev Cell. 2001; 1(4):527-37. DOI: 10.1016/s1534-5807(01)00063-6. View

12.

Hamburger Z, Hamburger A, West Jr A, Weis W . Crystal structure of the S.cerevisiae exocyst component Exo70p. J Mol Biol. 2005; 356(1):9-21. DOI: 10.1016/j.jmb.2005.09.099. View

13.

Mima J, Hickey C, Xu H, Jun Y, Wickner W . Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. EMBO J. 2008; 27(15):2031-42. PMC: 2516887. DOI: 10.1038/emboj.2008.139. View

14.

Wiederkehr A, De Craene J, 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; 167(5):875-87. PMC: 2172455. DOI: 10.1083/jcb.200408001. View

15.

Boyd C, Hughes T, Pypaert M, Novick P . Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J Cell Biol. 2004; 167(5):889-901. PMC: 2172445. DOI: 10.1083/jcb.200408124. View

16.

Wedlich-Soldner R, Altschuler S, Wu L, Li R . Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science. 2003; 299(5610):1231-5. DOI: 10.1126/science.1080944. View

17.

Hattendorf D, Andreeva A, Gangar A, Brennwald P, Weis W . Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism. Nature. 2007; 446(7135):567-71. DOI: 10.1038/nature05635. View

18.

Hsu S, Ting A, Hazuka C, Davanger S, KENNY J, Kee Y . The mammalian brain rsec6/8 complex. Neuron. 1996; 17(6):1209-19. DOI: 10.1016/s0896-6273(00)80251-2. View

19.

Songer J, Munson M . Sec6p anchors the assembled exocyst complex at sites of secretion. Mol Biol Cell. 2008; 20(3):973-82. PMC: 2633393. DOI: 10.1091/mbc.e08-09-0968. View

20.

Novick P, Field C, Schekman R . Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 1980; 21(1):205-15. DOI: 10.1016/0092-8674(80)90128-2. View