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TitleCryo-EM structure of the human Derlin-1/p97 complex reveals a hexameric channel in ERAD.
Journal, issue, pagesCommun Biol, Vol. 8, Issue 1, Page 1481, Year 2025
Publish dateOct 17, 2025
AuthorsQian Wang / Deqiang Yao / Bing Rao / Ying Xia / Wenguo Li / Shaobai Li / Mi Cao / Yafeng Shen / An Qin / Yu Cao /
PubMed AbstractThe ER-associated degradation (ERAD) pathway retrotranslocates misfolded proteins from the ER lumen to the cytoplasm for proteasomal degradation. Derlin-1 and p97 are central to this process, forming ...The ER-associated degradation (ERAD) pathway retrotranslocates misfolded proteins from the ER lumen to the cytoplasm for proteasomal degradation. Derlin-1 and p97 are central to this process, forming a canonical 4:6 complex with tetrameric Derlin-1. Using cryo-electron microscopy, we identify a novel human Derlin-1/p97 complex with a 6:6 stoichiometry, where hexameric Derlin-1 assembles as three dimers. This hexameric channel forms a significantly larger trans-ER membrane tunnel, potentially accommodating bulkier substrates. Structural comparisons revealed conformational flexibility in Derlin-1, suggesting the "U"-shaped tetramer may act as an intermediate in hexamer formation. The formation of this hexameric channel is mediated by interactions with p97 and appears dependent on p97's ATPase activity, which provides the driving force for the transition between the tetrameric channel conformation to the intermediate "U"-shaped conformation. These findings highlight the dynamic nature of the Derlin-1/p97 complex and its implications for understanding ERAD retrotranslocation.
External linksCommun Biol / PubMed:41107410 / PubMed Central
MethodsEM (single particle)
Resolution3.55 Å
Structure data

63205

9llk

EMDB-63205, PDB-9llk:
The cryo-EM structure of the heterododecameric human Derlin-1/p97 complex
Method: EM (single particle) / Resolution: 3.55 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ERAD

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