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The structure of the COPI coat determined within the cell. | LitMetric

The structure of the COPI coat determined within the cell.

Elife

Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.

Published: November 2017

AI Article Synopsis

  • COPI-coated vesicles play a crucial role in transporting materials within the Golgi apparatus and to the endoplasmic reticulum, and their structures have been studied using purified components.
  • Recent research utilized advanced imaging techniques to reveal the native structure of the COPI coat in cells, showing similarities to mammalian structures while identifying unique cargo arrangements.
  • The study found that all components of the COPI coat disassemble quickly after vesicle budding, but the overall structure of the coat mechanism remains consistent despite changes in vesicle size, membrane thickness, and cargo content during transport.

Article Abstract

COPI-coated vesicles mediate trafficking within the Golgi apparatus and from the Golgi to the endoplasmic reticulum. The structures of membrane protein coats, including COPI, have been extensively studied with reconstitution systems using purified components. Previously we have determined a complete structural model of the reconstituted COPI coat (Dodonova et al., 2017). Here, we applied cryo-focused ion beam milling, cryo-electron tomography and subtomogram averaging to determine the native structure of the COPI coat within vitrified cells. The native algal structure resembles the mammalian structure, but additionally reveals cargo bound beneath β'-COP. We find that all coat components disassemble simultaneously and relatively rapidly after budding. Structural analysis , maintaining Golgi topology, shows that vesicles change their size, membrane thickness, and cargo content as they progress from to , but the structure of the coat machinery remains constant.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5716667PMC
http://dx.doi.org/10.7554/eLife.32493DOI Listing

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