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Article

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.

Nature cell biology - 1 Mar 2008

Christianson John C, Shaler Thomas A, Tyler Ryan E, Kopito Ron R

Abstract excerpt

Terminally misfolded or unassembled proteins in the early secretory pathway are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). How substrates of this pathway are recognized within the ER and delivered to the cytoplasmic ubiquitin-conjugating machinery is unknown. We report here that OS-9 and XTP3-B/Erlectin are ER-resident glycoproteins that bind to ERAD...

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Identifiers

PMID: 18264092
DOI: 10.1038/ncb1689
PMCID: PMC2757077

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.PMID 18264092Read ↗

Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core ComplexSemantic proximity Read ↗

Structural basis and pathological implications of the dimeric OS9-SEL1L-HRD1 ERAD Core Complex.Semantic proximity Read ↗

The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.Semantic proximity Read ↗

Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.Semantic proximity Read ↗

The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.Semantic proximity Read ↗

SEL1L-HRD1 interaction is prerequisite for the formation of a functional HRD1 ERAD complexSemantic proximity Read ↗

ER-to-lysosome-associated degradation acts as failsafe mechanism upon ERAD dysfunctionSemantic proximity Read ↗

Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate.Semantic proximity Read ↗

Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Semantic proximity Read ↗

Mechanisms of transmembrane domain recognition during endoplasmic reticulum quality controlSemantic proximity Read ↗

Functional integrity of the SEL1L-HRD1 complex is critical for ERAD and organismal viabilitySemantic proximity Read ↗

Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase.Semantic proximity Read ↗

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