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Mutation of the Srpk79D gene causes conspicuous accumulations of BRP (show GDF5 Proteins) in larval and adult nerves.
SRPK79D is a novel T-bar-associated protein kinase (show CDK7 Proteins) that represses T-bar assembly in peripheral axons, and that SRPK79D-dependent repression must be relieved to facilitate site-specific AZ assembly.
In 2 independent murine models of breast tumor metastasis, stable shRNA-based SRPK1 knockdown suppressed metastasis to distant organs, including lung, liver, and spleen, and inhibited focal adhesion reorganization.
SRPK1 overexpression is also tumorigenic because excess SRPK1 squelches PHLPP1.
SRPK1 expression might be an important prognostic indicator for the chemoresponsiveness of nonseminomatous male germ cell tumors.
Findings suggest MALAT1 increases AKAP-9 expression by promoting SRPK1-catalyzed SRSF1 (show SRSF1 Proteins) phosphorylation in CRC (show CALR Proteins) cells. These results reveal a novel molecular mechanism by which MALAT1 regulates AKAP-9 expression in CRC (show CALR Proteins) cells.
The frameshift mutation detected in the current study would result in premature stops of amino acid synthesis in PLA2R1 (show PLA2R1 Proteins) and SRPK1 proteins and hence resembles a typical inactivating mutation.
Data suggest that ERH interacts directly in nucleus with C-terminal Arg-Gly-rich region of SAFB1/SAFB2 and this multimer co-localizes in insoluble nuclear fraction; binding of ERH reverses inhibition exerted by SAFB1/SAFB2 on SRPK1. (ERH = enhancer of rudimentary homolog protein; SAFB = scaffold attachment factor B; SRPK1 = splicing kinase SR protein kinase-1)
SRPK1 interacts with an RS-like domain in the N terminus of CLK1 (show CDK11B Proteins) to facilitate the release of phosphorylated SR proteins, which then promotes efficient splice-site recognition and subsequent spliceosome assembly.
Data indicate that proto-oncogene (show RAB1A Proteins) protein c (show PROC Proteins)-akt (Akt (show AKT1 Proteins)) phosphorylates distinct sites than SRPK1 protein within the arginine-serine (RS) domain of Lamin B Receptor (LBR (show LBR Proteins)).
SRPK1 interference inhibits the growth and invasion of RCC (show XRCC1 Proteins) cells.
SRPK1 is overexpressed in HCC (show FAM126A Proteins) and may be a promising indicator of prognosis for HCC (show FAM126A Proteins) patients
Overexpression of SRPK1 is associated with glioma.
The mRNA level and the protein level of SRPK1 were up-regulated in NSCLC tissues. It activated the transcriptional activity of beta-catenin/T-cell factor complex. SRPK1 knockdown attenuated the expression of target genes of this complex. Silencing SRPK1 down-regulated the phosphorylation of GSK3beta.
SRPK1 is upregulated in prostate cancer and correlates with disease stage and invasion.
This gene encodes a serine/arginine protein kinase specific for the SR (serine/arginine-rich domain) family of splicing factors. The protein localizes to the nucleus and the cytoplasm. It is thought to play a role in regulation of both constitutive and alternative splicing by regulating intracellular localization of splicing factors. Alternative splicing of this gene results in multiple transcript variants. Additional alternatively spliced transcript variants have been described for this gene, but their full length nature have not been determined.
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, serine/arginine-rich protein specific kinase 1
, SRSF protein kinase 1
, SFRS protein kinase 1
, SR protein-specific kinase 1
, SR-protein-specific kinase 1
, serine/arginine-rich protein-specific kinase 1
, serine/threonine-protein kinase SRPK1
, serine/arginine-rich splicing factor kinase 1
, Serine/threonine-protein kinase SRPK1