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-Structure paper
タイトル | Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 2034, Year 2021 |
掲載日 | 2021年4月1日 |
著者 | Joshua Hutchings / Viktoriya G Stancheva / Nick R Brown / Alan C M Cheung / Elizabeth A Miller / Giulia Zanetti / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:33795673 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 4.6 - 40.0 Å |
構造データ | EMDB-11193, PDB-6zg5: EMDB-11194, PDB-6zg6: EMDB-11197: EMDB-11198: EMDB-11199, PDB-6zga: EMDB-11264, PDB-6zl0: |
化合物 | ChemComp-HOH: ChemComp-ZN: ChemComp-GNP: ChemComp-MG: |
由来 |
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キーワード | PROTEIN TRANSPORT / SECRETION / TRAFFICKING |