Regulating SR protein phosphorylation through regions outside the kinase domain of SRPK1.

ABSTRACT: SR proteins (splicing factors containing arginine-serine repeats) are essential splicing factors whose phosphorylation by the SR-specific protein kinase (SRPK) family regulates nuclear localization and mRNA processing activity. In addition to an N-terminal extension with unknown function, SRPKs contain a large, nonhomologous spacer insert domain (SID) that bifurcates the kinase domain and anchors the kinase in the cytoplasm through interactions with chaperones. While structures for the kinase domain are now available, constructs that include regions outside this domain have been resistant to crystallographic elucidation. To investigate the conformation of the full-length kinase and the functional role of noncatalytic regions, we performed hydrogen-deuterium exchange and steady-state kineti

SUBMITTER: Plocinik RM 

PROVIDER: S-EPMC3121894 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature