Structure of the ER membrane complex, a transmembrane-domain insertase

The endoplasmic reticulum (ER) membrane complex (EMC) cooperates with the Sec61 translocon to co-translationally insert a transmembrane helix (TMH) of many multi-pass integral membrane proteins into the ER membrane, and it is also responsible for inserting the TMH of some tail-anchored proteins 1 –...

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Veröffentlicht in:	Nature (London) Jg. 584; H. 7821; S. 475 - 478
Hauptverfasser:	Bai, Lin, You, Qinglong, Feng, Xiang, Kovach, Amanda, Li, Huilin
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	London Nature Publishing Group UK 20.08.2020 Nature Publishing Group
Schlagworte:	101/28 101/58 14/19 631/45/173 631/535/1258/1259 631/80/2023/2022 82/16 82/83 Binding Sites Conservation Cryoelectron Microscopy Electron microscopy Endoplasmic reticulum Endoplasmic Reticulum - chemistry Endoplasmic Reticulum - enzymology Endoplasmic Reticulum - ultrastructure Evolution, Molecular Evolutionary conservation Humanities and Social Sciences Hydrophobic and Hydrophilic Interactions Insertion Integral membrane proteins Integrals Intracellular Membranes - chemistry Intracellular Membranes - enzymology Intracellular Membranes - ultrastructure Membranes Microscopy Models, Molecular multidisciplinary Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Multiprotein Complexes - ultrastructure Mutation Protein Domains Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Proteins Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Science Science (multidisciplinary) Structure-function relationships Substrate Specificity Transmembrane domains Yeast
ISSN:	0028-0836, 1476-4687, 1476-4687
Online-Zugang:	Volltext
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