SRPK1 is a Ser/Thr protein kinase that has sequence and function similar to SRPK2. In human cancer cells, it was observed that inactivation of SRPK1 induces cellular resistance to anticancer drugs such as cisplatin and bleomycin. SRPK1 phosphorylates serine/arginine-rich (SR) proteins, such as splicing factors ASF/SF2, SC35, and SRp55, in their arginine/serine-rich (RS) domains in vitro. Hence it is believed that SRPK1 plays a key role in regulation of both constitutive and alternative splicing by regulating intracellular localization of splicing factors.
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Aberrant patterns of pre-mRNA processing are typical of human malignancies, yet the mechanisms responsible for these changes remain undefined. We have recently shown overexpression of a core splice regulatory protein, serine-arginine protein kinase 1 (SRPK1), in dysplastic and neoplastic pancreatic
Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP splicing factors containing a serine/arginine-rich domain (SR proteins) concentrate in 'speckles' in the nucleus of interphase cells. It is believed that nuclear speckles act as storage sites for splicing factors while splicing occurs
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