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Article

Systematic Characterization of Cancer-Associated SPOP Mutants Reveals Novel and Reprogrammable Degradative Activities.

Chembiochem : a European journal of chemical biology - 1 Jan 2026

Caldwell Alana G, Parmar Harshil, Jin Xiaokang, Zhou Chen, Zhang Xiaoyu

Abstract excerpt

Speckle-type POZ protein (SPOP) functions as the substrate adaptor of the Cullin3-RING ligase complex and is recurrently mutated in multiple cancer types. Among these, F102C and F133L are frequent prostate cancer mutations within the substrate-binding domain, yet their biochemical consequences remain incompletely understood. Using quantitative proteomics, we show that SPOP-F133L, unlike SPOP-F102C, retains...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 41532714
DOI: 10.1002/cbic.202500914
PMCID: PMC12802387

Genes

SPOP
NUP153
TPR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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Systematic Characterization of Cancer-Associated SPOP Mutants Reveals Novel and Reprogrammable Degradative Activities.PMID 41532714Read ↗

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Prostate cancer-associated mutation in SPOP impairs its ability to target Cdc20 for poly-ubiquitination and degradation.Semantic proximity Read ↗

Functional dissection of <i>SPOP</i> on the amino acid level reveals a comprehensive functional landscape of variants during tumorigenesisSemantic proximity Read ↗

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SPOP Mutations Target STING1 Signaling in Prostate Cancer and Create Therapeutic Vulnerabilities to PARP Inhibitor-Induced Growth Suppression.Semantic proximity Read ↗

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