Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.

The Journal of cell biology - 27 Apr 2015

Habeck Gregor, Ebner Felix A, Shimada-Kreft Hiroko, Kreft Stefan G

Abstract excerpt

Aberrant endoplasmic reticulum (ER) proteins are eliminated by ER-associated degradation (ERAD). This process involves protein retrotranslocation into the cytosol, ubiquitylation, and proteasomal degradation. ERAD substrates are classified into three categories based on the location of their degradation signal/degron: ERAD-L (lumen), ERAD-M (membrane), and ERAD-C (cytosol) substrates. In Saccharomyces cerevisiae,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytosol
Share to Endoplasmic Reticulum-Associated Degradation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunoblotting

Share to Membrane Transport Proteins

Share to Microscopy, Fluorescence

Share to SEC Translocation Channels

Share to Ubiquitin

Share to Ubiquitin-Protein Ligases

Source

Open in PubMed Open full text

Identifiers

PMID: 25918226
DOI: 10.1083/jcb.201408088
PMCID: PMC4411271

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.PMID 25918226Read ↗

Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.Semantic proximity Read ↗

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

Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways.Semantic proximity Read ↗

Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases.Semantic proximity Read ↗

Proteome-wide C-degron activity profiling connects conditional regulation of the CTLH E3 ligase complex to ribosome biogenesisSemantic proximity Read ↗

The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.Semantic proximity Read ↗

A role for mammalian Ubc6 homologues in ER-associated protein degradation.Semantic proximity Read ↗

Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins.Semantic proximity Read ↗

Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD).Semantic proximity Read ↗

A positive genetic selection for transmembrane domain mutations in HRD1 underscores the importance of Hrd1 complex integrity during ERAD.Semantic proximity Read ↗

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

A 'distributed degron' allows regulated entry into the ER degradation pathway.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.