The exocyst defrocked, a framework of rods revealed
Abstract
The exocyst complex is required for the interaction of vesicles with the plasma membrane in preparation for exocytic fusion. Recent crystallographic studies indicate that at least four of the eight subunits contain long, rod-like domains formed from helical bundles. These rods may pack against one another to generate the framework of the complex. How this complex assembles, how it responds to various GTPases and how it is ultimately displaced to allow bilayer fusion are key questions for the future.
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The exocyst is a protein complex that can govern the polarized cell-surface delivery of membrane and membrane proteins.
“The exocyst is a protein complex that can govern the polarized cell-surface delivery of membrane and membrane proteins (Munson and Novick, 2006;Wu et al, 2008;He and Guo, 2009;Jin et al, 2011).”
From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Munson and Novick, 2006
Cites
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417 · cited 1× · see citing works
“In both examples, cargo is selected and vesicles are budded either from the trans-Golgi network or from recycling endosomes (1) and transported to sites of secretion on the plasma membrane (2), where they are tethered by the exocyst complex (3).”
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Endocytosis and Autophagy: Exploitation or Cooperation?
Tooze, S. A., Abada, A., & Elazar, Z. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018358 · Cited by 202 · see citing works
Cryo-EM structure of the exocyst complex
Mei, K., Li, Y., Wang, S., Shao, G., Wang, J., Ding, Y., Luo, G., Yue, P., Liu, J.-J., Wang, X., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0016-2 · Cited by 156 · see citing works
Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst
Teodoro, R. O., Pekkurnaz, G., Nasser, A., Higashi‐Kovtun, M. E., Balakireva, M., McLachlan, I. G., Camonis, J., & Schwarz, T. L. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.147 · Cited by 61 · see citing works
- Authors
- Munson, M., & Novick, P.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Yale University (US)
- Corresponding author
- Munson, Mary
- Novick, Peter
- Venue
- Nature Structural & Molecular Biology
- Published
- 2006-07
- Volume
- 13
- Issue
- 7
- Pages
- 577-581
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2057685812
- Cited by
- 290
- References
- 1
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 12 · 2023: 4 · 2022: 6 · 2021: 10 · 2020: 8 · 2019: 11 · 2018: 7 · 2017: 16 · 2016: 5 · 2015: 20 · 2014: 16 · 2013: 30 · 2012: 29
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (P01CA046128, CA46128)
- National Institute of General Medical Sciences (R01GM068803, GM-068803, GM 35370)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- exocyst complex, exocytosis, vesicle fusion, plasma membrane, crystal structure, helical bundle, protein complex formation, GTPase, membrane trafficking
- MeSH terms
- Animals, Exocytosis, Models, Molecular, Nucleic Acid Conformation, RNA, Cell Membrane Structures
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