{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rajecky M"],"funding":["Deutsche Forschungsgemeinschaft","MEYS","Czech-BioImaging large RI","Bader Philanthropies","Czech Science Foundation","e-INFRA CZ","National Infrastructure for Chemical Biology"],"pagination":["gkaf1343"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12721332"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(22)"],"pubmed_abstract":["Cyclin-dependent kinase 11 (CDK11) is essential for the regulation of pre-mRNA splicing via phosphorylation of the core spliceosome component SF3B1. This phosphorylation is a marker of the catalytically active spliceosomes; thus, it is important to identify the mechanisms that regulate CDK11 itself. Here, we report that a small subset of CDK11 is phosphorylated on the activation T-loop threonine 595 (Thr595) and is associated with the activated spliceosome on chromatin in gene bodies. Mutational analyses revealed that Thr595 is essential for the formation of the active CDK11 complex with cyclin L and SAP30BP. CDK11 transiently associates with CDK7, a transcriptional kinase that also promotes the activation of other CDKs. Inhibition of CDK7 initially decreases transcription, but longer dura"],"journal":["Nucleic acids research"],"pubmed_title":["CDK7-CDK11 axis in spliceosome regulation and pre-mRNA splicing."],"pmcid":["PMC12721332"],"funding_grant_id":["23-04754X","CZ-OPENSCREEN LM2023052","LM2023042","ID:90254","443644894","FR 2938/11-1","LM2023050"],"pubmed_authors":["Gajduskova P","Hegedusova E","Rajecky M","Martinkova P","Paruch K","Manik P","Zdrahal Z","Krystofova K","Hluchy M","Slaba Z","Sebesta M","Blazek D","Friedel CC","Khirsariya P","Potesil D"],"additional_accession":[]},"is_claimable":false,"name":"CDK7-CDK11 axis in spliceosome regulation and pre-mRNA splicing.","description":"Cyclin-dependent kinase 11 (CDK11) is essential for the regulation of pre-mRNA splicing via phosphorylation of the core spliceosome component SF3B1. This phosphorylation is a marker of the catalytically active spliceosomes; thus, it is important to identify the mechanisms that regulate CDK11 itself. Here, we report that a small subset of CDK11 is phosphorylated on the activation T-loop threonine 595 (Thr595) and is associated with the activated spliceosome on chromatin in gene bodies. Mutational analyses revealed that Thr595 is essential for the formation of the active CDK11 complex with cyclin L and SAP30BP. CDK11 transiently associates with CDK7, a transcriptional kinase that also promotes the activation of other CDKs. Inhibition of CDK7 initially decreases transcription, but longer dura","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-07-02T03:11:29.35Z","creation":"2026-07-02T03:08:35.252Z"},"accession":"S-EPMC12721332","cross_references":{"pubmed":["41428738"],"doi":["10.1093/nar/gkaf1343"]}}