{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Franz A"],"funding":["Deutsche Forschungsgemeinschaft","Boehringer Ingelheim Fonds"],"pagination":["e202201826"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9772828"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(3)"],"pubmed_abstract":["Regulation and functionality of species-specific alternative splicing has remained enigmatic to the present date. Calcium/calmodulin-dependent protein kinase IIβ (CaMKIIβ) is expressed in several splice variants and plays a key role in learning and memory. Here, we identify and characterize several primate-specific <i>CAMK2B</i> splice isoforms, which show altered kinetic properties and changes in substrate specificity. Furthermore, we demonstrate that primate-specific <i>CAMK2B</i> alternative splicing is achieved through branch point weakening during evolution. We show that reducing branch point and splice site strengths during evolution globally renders constitutive exons alternative, thus providing novel mechanistic insight into <i>cis</i>-directed species-specific alternative splicing"],"journal":["Life science alliance"],"pubmed_title":["Branch point strength controls species-specific <i>CAMK2B</i> alternative splicing and regulates LTP."],"pmcid":["PMC9772828"],"funding_grant_id":["278001972"],"pubmed_authors":["Kuropka B","Voigt A","Urlaub H","Franz A","Neumann A","Wahl MC","Heyd F","Dimos N","Schmitz D","Schulz F","Preußner M","Ji Y","Weber AI","Moreno-Velasquez L","Stumpf A","Kuhn R"],"additional_accession":[]},"is_claimable":false,"name":"Branch point strength controls species-specific <i>CAMK2B</i> alternative splicing and regulates LTP.","description":"Regulation and functionality of species-specific alternative splicing has remained enigmatic to the present date. Calcium/calmodulin-dependent protein kinase IIβ (CaMKIIβ) is expressed in several splice variants and plays a key role in learning and memory. Here, we identify and characterize several primate-specific <i>CAMK2B</i> splice isoforms, which show altered kinetic properties and changes in substrate specificity. Furthermore, we demonstrate that primate-specific <i>CAMK2B</i> alternative splicing is achieved through branch point weakening during evolution. We show that reducing branch point and splice site strengths during evolution globally renders constitutive exons alternative, thus providing novel mechanistic insight into <i>cis</i>-directed species-specific alternative splicing","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2026-05-27T19:14:26.03Z","creation":"2025-05-18T12:49:01.282Z"},"accession":"S-EPMC9772828","cross_references":{"pubmed":["36543542"],"doi":["10.26508/lsa.202201826"]}}