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

Conserved Mitotic Phosphorylation of a Proteasome Subunit Regulates Cell Proliferation.

Cells - 8 Nov 2021

Duan Jinyuan, Li Wenzhu, Shu Xin, Yang Bing, He Xiangwei, Guo Xing

Abstract excerpt

Reversible phosphorylation has emerged as an important mechanism for regulating proteasome function in various physiological processes. Essentially all proteasome phosphorylations characterized thus far occur on proteasome holoenzyme or subcomplexes to regulate substrate degradation. Here, we report a highly conserved phosphorylation that only exists on the unassembled α5 subunit of the proteasome. The modified...

Read the complete abstract on PubMed

Topics

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

Share to Cell Cycle Proteins
Share to Conserved Sequence
Share to Mitosis

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

Share to Phosphoserine

Share to Polo-Like Kinase 1

Share to Proteasome Endopeptidase Complex

Share to Protein Interaction Maps

Share to Protein Subunits

Source

Open in PubMed Open full text

Identifiers

PMID: 34831298
DOI: 10.3390/cells10113075
PMCID: PMC8620773

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

Conserved Mitotic Phosphorylation of a Proteasome Subunit Regulates Cell Proliferation.PMID 34831298Read ↗

CDK1-mediated mitotic phosphorylation of PBK is involved in cytokinesis and inhibits its oncogenic activity.Semantic proximity Read ↗

Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-dependent kinase Cdk1.Semantic proximity Read ↗

Quantitative kinase and phosphatase profiling reveal that CDK1 phosphorylates PP2Ac to promote mitotic entry.Semantic proximity Read ↗

Polo-like kinase 1 (PLK1) O-GlcNAcylation is essential for dividing mammalian cells and inhibits uterine carcinoma.Semantic proximity Read ↗

ASPP2 Is Phosphorylated by CDK1 during Mitosis and Required for Pancreatic Cancer Cell ProliferationSemantic proximity Read ↗

Quantitative phosphoproteomics reveals regulatory state dependent efficacy of chemical Cdk1 inhibition and distinct Cdk5 complexes as novel Wee1 substratesSemantic proximity Read ↗

The roles, molecular interactions, and therapeutic value of CDK16 in human cancersSemantic proximity Read ↗

Mitotic arrest-induced phosphorylation of Mcl-1 revisited using two-dimensional gel electrophoresis and phosphoproteomics: nine phosphorylation sites identified.Semantic proximity Read ↗

A cell cycle phosphoproteome of the yeast centrosome.Semantic proximity Read ↗

Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover.Semantic proximity Read ↗

Key phosphorylation events in Spc29 and Spc42 guide multiple steps of yeast centrosome duplication.Semantic proximity Read ↗

Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.Semantic proximity Read ↗

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