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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SRSF protein kinase 2

Top mentioned proteins: SRPK1, CAN, Akt, FATE, V1a
Papers on SRPK2
Alternative splicing of the cell fate determinant Numb in hepatocellular carcinoma.
Neckers et al., Beijing, China. In Hepatology, Oct 2015
In the cell models explored in this study, alternative splicing of Numb PRR isoforms is coordinately regulated by the splicing factor RNA-binding Fox domain containing 2 (RbFox2) and the kinase serine/arginine protein-specific kinase 2 (SRPK2).
Increased Serine-Arginine (SR) Protein Phosphorylation Changes Pre-mRNA Splicing in Hypoxia.
Kanopka et al., Vilnius, Lithuania. In J Biol Chem, Aug 2015
We also show that expression of SR protein kinases (CLK1, SRPK1, SRPK2) in hypoxic cells is elevated at mRNA and protein levels.
Potential Antileukemia Effect and Structural Analyses of SRPK Inhibition by N-(2-(Piperidin-1-yl)-5-(Trifluoromethyl)Phenyl)Isonicotinamide (SRPIN340).
Bressan et al., Viçosa, Brazil. In Plos One, 2014
Previous investigations have described the overexpression of SRPK1 and SRPK2 in leukemia and other cancer types, suggesting that they would be useful targets for developing novel antitumor strategies.
Primary structural features of SR-like protein acinusS govern the phosphorylation mechanism by SRPK2.
Ngo et al., Hong Kong, Hong Kong. In Biochem J, 2014
SRPK2 is highly related to SRPK1 in sequence and in vitro properties, yet it has been shown to have distinct substrate specificity and physiological function in vivo.
Paraquat modulates alternative pre-mRNA splicing by modifying the intracellular distribution of SRPK2.
Barabino et al., Milano, Italy. In Plos One, 2012
We show that PQ treatment leads to the phosphorylation and nuclear accumulation of SRPK2, a member of the family of serine/arginine (SR) protein-specific kinases.
An RS motif within the Epstein-Barr virus BLRF2 tegument protein is phosphorylated by SRPK2 and is important for viral replication.
Johannsen et al., Boston, United States. In Plos One, 2012
Serine/Arginine-rich Protein Kinase 2 (SRPK2) was identified by both assays and was further shown to phosphorylate an RS motif in the BLRF2 C-terminus.
Serine-arginine protein kinases: new players in neurodegenerative diseases?
Ye et al., In Rev Neurosci, 2012
Our recent studies demonstrate that one of the SRPK members, SRPK2, participates in the neuronal survival, cell cycle progression, and memory determination in Alzheimer's disease.
SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease.
Ye et al., Atlanta, United States. In J Neurosci, 2012
Serine-arginine protein kinases 2 (SRPK2) is a cell cycle-regulated kinase that phosphorylates serine/arginine domain-containing proteins and mediates pre-mRNA splicing with unclear function in neurons.
Abnormal expression of the pre-mRNA splicing regulators SRSF1, SRSF2, SRPK1 and SRPK2 in non small cell lung carcinoma.
Eymin et al., Grenoble, France. In Plos One, 2011
Consistently, we further show that the SR-phosphorylating kinases SRPK1 and SRPK2 are upregulated in 92% and 94% of ADC as well as in 72% and 68% of SCC, respectively.
Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin.
Eymin et al., Grenoble, France. In Embo J, 2011
In addition, we show that Tip60 downregulates SRSF2 phosphorylation by inhibiting the nuclear translocation of both SRPK1 and SRPK2 kinases.
The N-terminal fragment from caspase-cleaved serine/arginine protein-specific kinase2 (SRPK2) translocates into the nucleus and promotes apoptosis.
Ye et al., Atlanta, United States. In J Biol Chem, 2011
SRPK2 belongs to a family of serine/arginine (SR) protein-specific kinases (SRPKs), which phosphorylate SR domain-containing proteins in the nuclear speckles and mediate the pre-mRNA splicing.
Inhibition of hepatitis C virus replication by a specific inhibitor of serine-arginine-rich protein kinase.
Watanabe et al., Tokyo, Japan. In Antimicrob Agents Chemother, 2010
Our results demonstrate that SRPK1 and SRPK2 are host factors essential for Hepatitis C virus replication.
3.2 Mb microdeletion in chromosome 7 bands q22.2-q22.3 associated with overgrowth and delayed bone age.
Renieri et al., Siena, Italy. In Eur J Med Genet, 2010
Four genes are implicated in the control of cell cycle: SRPK2, MLL5, RINT1 and LHFPL3.
Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons.
Ye et al., Atlanta, United States. In J Biol Chem, 2009
Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons.
Changed profile of splicing regulator genes expression in response to exercise.
Sakharov et al., Moscow, Russia. In Bull Exp Biol Med, 2009
Short-term exercise resulted in a significant increase of mRNA expression of genes encoding proteins involved in the formation of precatalytic splisosome: SRPK2.
Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1.
Ye et al., Atlanta, United States. In Cancer Res, 2008
overexpression of SRPK2 is associated with phosphorylating acinus and regulating its stimulatory effects on cyclin A1 expression, contributing to leukemia cell proliferation
Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome.
Lührmann et al., Göttingen, Germany. In Nat Struct Mol Biol, 2008
SRPK2 knock down results in hypophosphorylation of the arginine-serine (RS) domain-containing human PRP28 protein (PRP28, also known as DDX23), and destabilizes PRP28 association with the tri-snRNP.
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