Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex

Misfolded luminal endoplasmic reticulum (ER) proteins undergo ER-associated degradation (ERAD-L): They are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. ERAD-L is mediated by the Hrd1 complex (composed of Hrd1, Hrd3, Der1, Usa1, and Yos9), but the mechanism o...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2020-04, Vol.368 (6489)
Hauptverfasser:	Wu, Xudong, Siggel, Marc, Ovchinnikov, Sergey, Mi, Wei, Svetlov, Vladimir, Nudler, Evgeny, Liao, Maofu, Hummer, Gerhard, Rapoport, Tom A
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Adenosine triphosphatase Binding sites Biodegradation Carrier Proteins - chemistry Carrier Proteins - metabolism Channels Computer simulation Control systems Crosslinking Cryoelectron Microscopy Cytosol Cytotoxicity Degradation Domains Electron microscopy Endoplasmic reticulum Endoplasmic Reticulum - metabolism Endoplasmic Reticulum-Associated Degradation Gates Glycan Glycoproteins Glycosidases Grooves Homeostasis Homology Hydrophobicity Inserts Intermediates Lipids Macromolecules Mannose Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Membrane Proteins - chemistry Membrane Proteins - metabolism Membranes Microscopy Molecular dynamics Molecular Dynamics Simulation Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Phospholipids Polypeptides Proteasomes Protein Domains Protein Folding Protein transport Proteins Proteolysis Quality control Residues Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Substrates Translocation Triphosphatase Ubiquitin Ubiquitin-protein ligase Ubiquitin-Protein Ligases - chemistry Yeasts
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