PSKH1, a novel splice factor compartment‐associated serine kinase

摘要: Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP splicing factors containing a serine/arginine-rich domain (SR proteins) concentrate in factor compartments (SFCs) within the nucleus of interphase cells. Nuclear SFCs are considered mainly as storage sites for factors, supplying to active genes. The mechanisms controlling interaction various spliceosome constituents, dynamic nature SFCs, still poorly understood. We show here that endogenous PSKH1, previously cloned kinase, is located SFCs. Migration PSKH1-FLAG into enhanced during co-expression T7-tagged ASF/SF2 well other members SR protein family, but not by two non-SR proteins serving controls. Similar kinase overexpression PSKH1 led reorganization co-expressed T7-SC35 T7-ASF/SF2 more diffuse pattern. This redistribution was dependent on activity. Different from kinases, SFC-associating features were its catalytic C-terminus. Although no direct observed between any tested pull-down or yeast two-hybrid assays, forced expression shown stimulate distal an E1A minigene HeLa Moreover, GST-ASF/SF2 fusion phosphorylated suggesting indirect mechanism action proteins. Our data suggest mutual relationship proteins, they able target while modulates dynamics function factors.