Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network

Joshua Hutchings, Viktoriya G. Stancheva, Nick R. Brown, Alan C. M. Cheung, Elizabeth A. Miller, Giulia Zanetti (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)
2 Downloads (Pure)

Abstract

COPII mediates Endoplasmic Reticulum to Golgi trafficking of thousands of cargoes. Five essential proteins assemble into a two-layer architecture, with the inner layer thought to regulate coat assembly and cargo recruitment, and the outer coat forming cages assumed to scaffold membrane curvature. Here we visualise the complete, membrane-assembled COPII coat by cryo-electron tomography and subtomogram averaging, revealing the full network of interactions within and between coat layers. We demonstrate the physiological importance of these interactions using genetic and biochemical approaches. Mutagenesis reveals that the inner coat alone can provide membrane remodelling function, with organisational input from the outer coat. These functional roles for the inner and outer coats significantly move away from the current paradigm, which posits membrane curvature derives primarily from the outer coat. We suggest these interactions collectively contribute to coat organisation and membrane curvature, providing a structural framework to understand regulatory mechanisms of COPII trafficking and secretion.
Original languageEnglish
Article number2034
Number of pages13
JournalNature Communications
Volume12
DOIs
Publication statusPublished - 1 Apr 2021

Keywords

  • Coat complexes
  • Cryoelectron tomography
  • Transport carrier

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