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Article

Prostate cancer. Ubiquitylome analysis identifies dysregulation of effector substrates in SPOP-mutant prostate cancer.

Science (New York, N.Y.) - 3 Oct 2014

Theurillat Jean-Philippe P, Udeshi Namrata D, Errington Wesley J, Svinkina Tanya, Baca Sylvan C, Pop Marius, Wild Peter J, Blattner Mirjam, Groner Anna C, Rubin Mark A, Moch Holger, Prive Gilbert G, Carr Steven A, Garraway Levi A

Abstract excerpt

Cancer genome characterization has revealed driver mutations in genes that govern ubiquitylation; however, the mechanisms by which these alterations promote tumorigenesis remain incompletely characterized. Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset...

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Share to Carcinogenesis
Share to Chromosomal Proteins, Non-Histone

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neoplasm Invasiveness

Share to Oncogene Proteins

Share to Poly-ADP-Ribose Binding Proteins

Share to Proteasome Endopeptidase Complex

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Source

Open in PubMed Open full text

Identifiers

PMID: 25278611
DOI: 10.1126/science.1250255
PMCID: PMC4257137

Genes

SPOP
DEK
TRIM24

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

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Prostate cancer. Ubiquitylome analysis identifies dysregulation of effector substrates in SPOP-mutant prostate cancer.PMID 25278611Read ↗

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