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MAPK6 — NPY4R

Text-mined interactions from Literome

Bondzi et al., Cell Growth Differ 2000 (Carcinoma, Small Cell...) : In the present study, we have demonstrated that PP1 , a pharmacological inhibitor of Src kinases, blocked SCF mediated activation of mitogen activated protein ( MAP ) kinase , but it also inhibited Kit activation
Mannon et al., Biochem J 2000 (MAP Kinase Signaling System) : The Src-family tyrosine kinase inhibitor PP1 , as well as specific inhibition of the epidermal growth factor receptor tyrosine kinase ( EGFR TK ) by PD153035, also blocks PYY stimulation of MAPK
Gentili et al., Exp Gerontol 2000 : Moreover, the tyrosine phosphorylation and activation of MAPK was dependent on Src kinase, since PP1 ( 10 and 20microM ), a specific Src family tyrosine-kinase inhibitor, blocked PTH induced MAPK activation
Mitsuhashi et al., J Biol Chem 2003 (MAP Kinase Signaling System) : Therefore, using TC as a specific PP1 inhibitor, the biological effect of PP1 on MAPK signaling was examined
Salinthone et al., Am J Physiol Gastrointest Liver Physiol 2004 (Inflammation) : Expression of IL-1beta, IL-6, IL-8, and COX-2 mRNA was reduced by 30 microM PP1 , an Src family tyrosine kinase inhibitor, and by 25 microM SB-203580, a p38 MAPK inhibitor
Wu et al., J Neurochem 2004 : AMPA mediated neuroprotection is blocked by PP1 , an inhibitor of src family kinases, LY294002, a PI3-K inhibitor, or U0126, a MAPK kinase ( MEK ) inhibitor
Zhou et al., Toxicological sciences : an official journal of the Society of Toxicology 2005 : PP1 suppressed DON induced phosphorylation of the MAPK substrates c-jun, ATF-2, and p90 ( Rsk )
Ungefroren et al., Curr Cancer Drug Targets 2011 : Likewise, PP2 and PP1 but not SU6656 effectively blocked TGF-ß1 induced activation of Smad2 and p38 MAPK and partially suppressed Smad activation and transcriptional activity on TGF-ß/Smad-responsive reporters of a kinase-active TßRI mutant ectopically expressed in Panc1 cells
Begum et al., Metabolism 1998 (Diabetes Mellitus, Type 2...) : We conclude that ( 1 ) a rapid activation of PP-1 along with concomitant inhibition of cytosolic PP-2A may be important in the mechanism of insulin action in a normal cell, and ( 2 ) the resistance to insulin in terms of glucose uptake and glycogen synthesis observed in diabetic GK rats is partly due to defective regulation of PP-1, PP-2A, and MAPK caused by multiple defects in the upstream insulin signaling components ( IRS-1/phosphatidylinositol-3-kinase [ PI3-kinase ] and Grb2/Sos ) that participate in insulin mediated activation of PP-1 and inactivation of PP-2A