Cryo-EM structure of the exocyst complex
Abstract
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 Å. 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.
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The model of the entire GARP complex shows the four subunits assemble through a four-helix bundle, with C-terminal 'CATCHR' folds in Vps52, Vps53, and Vps54 emanating from the bundle; this architecture resembles portions of the cryo-EM structure of the Exocyst complex.
“In this model, the four subunits assemble through a four-helix bundle. In each of the three larger subunits, Vps52, Vps53, and Vps54, C-terminal domains comprising “CATCHR” folds emanate from the bundle. This architecture resembles portions of the cryo-EM structure of the Exocyst complex, a distinct MTC that mediates fusion of vesicles at the plasma membrane (76), which possesses two separate four”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [76]
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Computed structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542 · see citing works
- Authors
- Mei, K., Li, Y., Wang, S., Shao, G., Wang, J., Ding, Y., Luo, G., Yue, P., Liu, J.-J., Wang, X., Dong, M.-Q., Wang, H.-W., & Guo, W.
- Affiliations
- University of Pennsylvania (US)
- Center for Life Sciences (CN)
- Tsinghua University (CN)
- National Institute of Biological Sciences, Beijing (CN)
- Corresponding author
- Guo, Wei
- Venue
- Nature Structural & Molecular Biology
- Published
- 2018-01-15
- Volume
- 25
- Issue
- 2
- Pages
- 139-146
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W4233003322
- Cited by
- 156
- References
- 74
- Citations by year
- 2026: 17 · 2025: 14 · 2024: 19 · 2023: 16 · 2022: 20 · 2021: 20 · 2020: 14 · 2019: 27 · 2018: 8
- FWCI
- 9.55
- Type
- journal article
- Language
- en
- Update notices
- correction (2018-11-05)
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM111128)
- 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 › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- exocyst complex, protein complex structure, vesicle tethering, exocytosis, secretory vesicles, plasma membrane, Saccharomyces cerevisiae, helical bundle, cell polarization, cytokinesis, ciliogenesis, tumor invasion
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