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

Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway.

Molecular cell - 23 May 2013

Shemorry Anna, Hwang Cheol-Sang, Varshavsky Alexander

Abstract excerpt

N(α)-terminal acetylation of cellular proteins was recently discovered to create specific degradation signals termed Ac/N-degrons and targeted by the Ac/N-end rule pathway. We show that Hcn1, a subunit of the APC/C ubiquitin ligase, contains an Ac/N-degron that is repressed by Cut9, another APC/C subunit and the ligand of Hcn1. Cog1, a subunit of the Golgi-associated COG complex, is also shown to contain an...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Adaptor Proteins, Vesicular Transport
Share to Golgi Apparatus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immunoblotting

Share to Protein Processing, Post-Translational

Share to Proteolysis

Share to Ubiquitin-Protein Ligases

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23603116
DOI: 10.1016/j.molcel.2013.03.018
PMCID: PMC3665649

Genes

APC

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway.PMID 23603116Read ↗

First Things First: Vital Protein Marks by N-Terminal Acetyltransferases.Semantic proximity Read ↗

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevitySemantic proximity Read ↗

NATs at a glanceSemantic proximity Read ↗

N-Terminal Acetylation Inhibits Protein Targeting to the Endoplasmic ReticulumSemantic proximity Read ↗

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevitySemantic proximity Read ↗

Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and RegulationSemantic proximity Read ↗

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humansSemantic proximity Read ↗

The <i>E. coli</i> sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sitesSemantic proximity Read ↗

NatF Contributes to an Evolutionary Shift in Protein N-Terminal Acetylation and Is Important for Normal Chromosome SegregationSemantic proximity Read ↗

Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.Semantic proximity Read ↗

C-terminal amides mark proteins for degradation via SCF/FBXO31Semantic proximity Read ↗

Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathwaySemantic proximity Read ↗

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