{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tian J"],"funding":["China Postdoctoral Science Foundation","Science and Technology Department of Henan Province (Henan Provincial Department of Science and Technology)","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["3625-3639"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12436196"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["44(38)"],"pubmed_abstract":["Centrosome amplification, a hallmark of diverse malignancies, enables cancer cell survival through centrosome clustering during mitosis, presenting a promising therapeutic target for selective elimination of cancer cells with supernumerary centrosomes. While the regulatory mechanisms underlying centrosome clustering remain poorly understood, our study identifies LIM kinase 2 (LIMK2) as a critical regulator of this process, demonstrating cancer correlation with tumor progression. Mechanistically, LIMK2 phosphorylates mammalian sterile-20-like kinase 4 (MST4) at threonine 178 (T178), activating its kinase function. Activated MST4 subsequently binds and phosphorylates nucleophosmin 1 (NPM1) at T95, a modification essential for centrosome clustering and tumor cell proliferation. Genetic deplet"],"journal":["Oncogene"],"pubmed_title":["LIMK2 promotes centrosome clustering and cancer progression by activating MST4-mediated phosphorylation of NPM1."],"pmcid":["PMC12436196"],"funding_grant_id":["242102311218","2023M733222","8207112153","82073075"],"pubmed_authors":["Tian J","Liu K","Song M","Zhang Y","Dong Z","Jia H","Yang R","Ge M","Liu S","Nie W"],"additional_accession":[]},"is_claimable":false,"name":"LIMK2 promotes centrosome clustering and cancer progression by activating MST4-mediated phosphorylation of NPM1.","description":"Centrosome amplification, a hallmark of diverse malignancies, enables cancer cell survival through centrosome clustering during mitosis, presenting a promising therapeutic target for selective elimination of cancer cells with supernumerary centrosomes. While the regulatory mechanisms underlying centrosome clustering remain poorly understood, our study identifies LIM kinase 2 (LIMK2) as a critical regulator of this process, demonstrating cancer correlation with tumor progression. Mechanistically, LIMK2 phosphorylates mammalian sterile-20-like kinase 4 (MST4) at threonine 178 (T178), activating its kinase function. Activated MST4 subsequently binds and phosphorylates nucleophosmin 1 (NPM1) at T95, a modification essential for centrosome clustering and tumor cell proliferation. Genetic deplet","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-03T03:02:26.092Z","creation":"2026-04-23T03:13:56.628Z"},"accession":"S-EPMC12436196","cross_references":{"pubmed":["40775397"],"doi":["10.1038/s41388-025-03518-6"]}}