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

Phosphorylation-dependent regulation of SPOP by LIMK2 promotes castration-resistant prostate cancer.

British journal of cancer - 1 Mar 2021

Nikhil Kumar, Haymour Hanan S, Kamra Mohini, Shah Kavita

Abstract excerpt

BACKGROUND: SPOP, an E3 ubiquitin ligase adaptor, can act either as a tumour suppressor or a tumour promoter. In prostate cancer (PCa), it inhibits tumorigenesis by degrading several oncogenic substrates. SPOP is the most altered gene in PCa (~15%), which renders it ineffective, promoting cancer. The remaining PCa tumours, which retain WT-SPOP, still progress to castration-resistant (CRPC) stage, indicating that...

Read the complete abstract on PubMed

Topics

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

Share to Cell Movement
Share to Lim Kinases
Share to Mice, Nude

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prostatic Neoplasms, Castration-Resistant

Share to Receptors, Androgen

Share to Repressor Proteins

Share to Ubiquitination

Share to Xenograft Model Antitumor Assays

Source

Open in PubMed Open full text

Identifiers

PMID: 33311589
DOI: 10.1038/s41416-020-01197-6
PMCID: PMC7921662

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation-dependent regulation of SPOP by LIMK2 promotes castration-resistant prostate cancer.PMID 33311589Read ↗

ERK1/2 inhibits Cullin 3/SPOP-mediated PrLZ ubiquitination and degradation to modulate prostate cancer progression.Semantic proximity Read ↗

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

SPOP-mediated ubiquitination and degradation of PDK1 suppresses AKT kinase activity and oncogenic functions.Semantic proximity Read ↗

Clinico-pathological significance of the molecular alterations of the SPOP gene in prostate cancer.Semantic proximity Read ↗

SPOP-mutant prostate cancer: Translating fundamental biology into patient care.Semantic proximity Read ↗

SPOP regulates prostate epithelial cell proliferation and promotes ubiquitination and turnover of c-MYC oncoprotein.Semantic proximity Read ↗

Androgen receptor is the key transcriptional mediator of the tumor suppressor SPOP in prostate cancer.Semantic proximity Read ↗

Dual functions of SPOP and ERG dictate androgen therapy responses in prostate cancer.Semantic proximity Read ↗

G3BP1 inhibits Cul3SPOP to amplify AR signaling and promote prostate cancer.Semantic proximity Read ↗

SPOP Gene Mutations in Prostate Cancer: Deciphering Their Role in Disease Characterization and Targeted Interventions on AR SignalingSemantic proximity Read ↗

SPOP mutations increase PARP inhibitor sensitivity via CK2/PIAS1/SPOP axis in prostate cancer.Semantic proximity Read ↗

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

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