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Article

Quality control autophagy degrades soluble ERAD-resistant conformers of the misfolded membrane protein GnRHR.

Molecular cell - 10 Apr 2014

Houck Scott A, Ren Hong Yu, Madden Victoria J, Bonner Jacob N, Conlin Michael P, Janovick Jo Ann, Conn P Michael, Cyr Douglas M

Abstract excerpt

Molecular chaperones triage misfolded proteins via action as substrate selectors for quality control (QC) machines that fold or degrade clients. Herein, the endoplasmic reticulum (ER)-associated Hsp40 JB12 is reported to participate in partitioning mutant conformers of gonadotropin-releasing hormone receptor (GnRHR), a G protein-coupled receptor, between ER-associated degradation (ERAD) and an ERQC autophagy...

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Identifiers

PMID: 24685158
DOI: 10.1016/j.molcel.2014.02.025
PMCID: PMC4070183

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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