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Cryo-EM structure of the exocyst complex.

Kunrong MeiYan LiShaoxiao WangGuangcan ShaoJia WangYuehe DingGuangzuo LuoPeng YueJun-Jie LiuXinquan WangMeng-Qiu DongHong-Wei WangWei Guo
Published in: Nature structural & molecular biology (2018)
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.
Keyphrases
  • single cell
  • saccharomyces cerevisiae
  • transcription factor
  • cell therapy
  • mass spectrometry
  • electronic health record
  • amino acid
  • bone marrow
  • mesenchymal stem cells
  • big data