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

Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control.

Proceedings of the National Academy of Sciences of the United States of America - 31 May 2011

Chen Meifan, Gutierrez Gustavo J, Ronai Ze'ev A

Abstract excerpt

The ubiquitin-recognition protein Ufd1 facilitates clearance of misfolded proteins through the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Here we report that prolonged ER stress represses Ufd1 expression to trigger cell cycle delay, which contributes to ERAD. Remarkably, down-regulation of Ufd1 enhances ubiquitination and destabilization of Skp2 mediated by the anaphase-promoting complex or...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Vesicular Transport
Share to Cell Cycle

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Separation

Share to Down-Regulation

Share to Endoplasmic Reticulum

Share to Gene Expression Regulation, Fungal

Share to S-Phase Kinase-Associated Proteins

Share to Tunicamycin

Source

Open in PubMed Open full text

Identifiers

PMID: 21571647
DOI: 10.1073/pnas.1100028108
PMCID: PMC3107271

Genes

APC
USP13

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control.PMID 21571647Read ↗

Emerging regulatory mechanisms in ubiquitin-dependent cell cycle controlSemantic proximity Read ↗

Deubiquitination of Chfr, a checkpoint protein, by USP7/HAUSP regulates its stability and activity.Semantic proximity Read ↗

Ubiquitin in Cell-Cycle Regulation and Dysregulation in CancerSemantic proximity Read ↗

Depletion of proteasome subunit PSMD1 induces cancer cell death via protein ubiquitination and DNA damage, irrespective of p53 statusSemantic proximity Read ↗

Regulation of Cyclin D1 Degradation by Ubiquitin-Specific Protease 27X Is Critical for Cancer Cell Proliferation and Tumor GrowthSemantic proximity Read ↗

A guide to UFMylation, an emerging posttranslational modificationSemantic proximity Read ↗

The Double Life of UPF1 in RNA and DNA Stability PathwaysSemantic proximity Read ↗

Comprehensive analysis of ubiquitin‐specific protease 1 reveals its importance in hepatocellular carcinomaSemantic proximity Read ↗

A balance of deubiquitinating enzymes controls cell cycle entrySemantic proximity Read ↗

Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response.Semantic proximity Read ↗

The NEDD8 Conjugation Pathway and Its Relevance in Cancer Biology and TherapySemantic proximity Read ↗

Skp1-Cul1-F-box ubiquitin ligase (SCF(βTrCP))-mediated destruction of the ubiquitin-specific protease USP37 during G2-phase promotes mitotic entry.Semantic proximity Read ↗

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