Cyclin-dependent kinase 1 (CDK1) and CDK2 have opposing roles in regulating interactions of splicing factor 3B1 with chromatin.

ABSTRACT: Splicing factor 3B1 (SF3B1) is a core splicing protein that stabilizes the interaction between the U2 snRNA and the branch point in the mRNA target during splicing. SF3B1 is heavily phosphorylated at its N terminus and a substrate of cyclin-dependent kinases (CDKs). Although SF3B1 phosphorylation coincides with splicing catalysis, the functional significance of SF3B1 phosphorylation is largely undefined. Here, we show that SF3B1 phosphorylation follows a dynamic pattern during cell cycle progression that depends on CDK activity. SF3B1 is known to interact with chromatin, and we found that SF3B1 maximally interacts with nucleosomes during G₁/S and that this interaction requires CDK2 activity. In contrast, SF3B1 disassociates from nucleosomes at G₂/M, coinciding with a

SUBMITTER: Murthy T 

PROVIDER: S-EPMC6028971 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature