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Nature structural & molecular biology
02, 2018;25 (2): 139-146.

Cryo-EM structure of the exocyst complex.

Kunrong Mei, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang, Yuehe Ding, Guangzuo Luo, Peng Yue, Jun-Jie Liu, Xinquan Wang, Meng-Qiu Dong, Hong-Wei Wang, Wei Guo
Author Information
  1. Kunrong Mei: Department of Biology, University of Pennsylvania, Philadelphia, PA, USA.
  2. Yan Li: Ministry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
  3. Shaoxiao Wang: Department of Biology, University of Pennsylvania, Philadelphia, PA, USA.
  4. Guangcan Shao: National Institute of Biological Sciences, Beijing, China.
  5. Jia Wang: Ministry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
  6. Yuehe Ding: National Institute of Biological Sciences, Beijing, China.
  7. Guangzuo Luo: Department of Biology, University of Pennsylvania, Philadelphia, PA, USA.
  8. Peng Yue: Department of Biology, University of Pennsylvania, Philadelphia, PA, USA.
  9. Jun-Jie Liu: Ministry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
  10. Xinquan Wang: Ministry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China.
  11. Meng-Qiu Dong: National Institute of Biological Sciences, Beijing, China. ORCID
  12. Hong-Wei Wang: Ministry of Education Key Laboratory of Protein Sciences, Tsinghua University, Beijing, China. hongweiwang@tsinghua.edu.cn.
  13. Wei Guo: Department of Biology, University of Pennsylvania, Philadelphia, PA, USA. guowei@sas.upenn.edu. ORCID
PMID: 29335562 DOI: 10.1038/s41594-017-0016-2

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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Grants

  1. R01 GM111128/NIGMS NIH HHS

MeSH Term

Amino Acid Motifs
Biological Transport
Cell Membrane
Cross-Linking Reagents
Cryoelectron Microscopy
Cytoplasm
Exocytosis
Golgi Apparatus
Image Processing, Computer-Assisted
Mass Spectrometry
Protein Binding
Protein Multimerization
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Secretory Vesicles
Vesicular Transport Proteins

Chemicals

Cross-Linking Reagents
Saccharomyces cerevisiae Proteins
Vesicular Transport Proteins
Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't
Article has an altmetric score of 18

Word Cloud

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