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F2R — SRC

Pathways - manually collected, often from reviews:

• Reactome Reaction: F2R → SRC (indirect_complex) Kuo et al., Cell Signal 2006, Luttrell et al., Science 1999*
• Reactome Reaction: F2R → SRC (reaction) Kuo et al., Cell Signal 2006, Luttrell et al., Science 1999*

Text-mined interactions from Literome

Sabri et al., Circ Res 2002 : Activation of PAR-1 leads to an increase in Src , Fyn, and epidermal growth factor receptor (EGFR) phosphorylation, with EGFR receptor transactivation by Src family kinases the major mechanism for PAR-1 dependent activation of extracellular signal regulated kinase, p38-mitogen activated protein kinase, and protein kinase B
Darmoul et al., Mol Cancer Res 2004 (Colonic Neoplasms) : Finally, PAR1 activation induces Src phosphorylation, which is reversed by using the Src tyrosine kinase inhibitor PP2, suggesting that Src activation plays a permissive role for PAR1 mediated ERK1/2 activation and cell proliferation probably acting downstream of the EGFR
Murugappan et al., Blood 2005 : Both PAR1 and PAR4 caused a time dependent activation of Src ( pp60c-src ) tyrosine kinase and Src tyrosine kinase inhibitors completely blocked the tyrosine phosphorylation of PKCdelta
Kuo et al., Cell Signal 2006 : Our results show that PAR1 mediated activation of Src and ERK1/2 in HEK 293 cells was increased with overexpression of beta-arrestin1 or depletion of beta-arrestin2 ... PAR1 mediated activation of Src and ERK1/2 in HEK 293 cells was decreased or eliminated with depletion of beta-arrestin1 or overexpression of beta-arrestin2 ... Furthermore, depletion of beta-arrestin2 blocked PAR1 induced degradation of Src ... Thus, beta-arrestin1 and beta-arrestin2 have opposing roles in regulating the activation of Src induced by PAR1 ... beta-Arrestin2 also appears to promote PAR1 induced degradation of Src
Lu et al., Cell Signal 2006 : Thus, PAR1 induced Src activation is negatively regulated by recruiting Csk through phosphocaveolin-1 ... The downregulation of PAR1 induced Src activation mediated by phosphocaveolin-1 provides an additional mechanism for the termination of PAR1 signaling at its downstream molecules
Sekiguchi et al., Biochem Pharmacol 2007 : The PAR1 activating peptide (PAR1-AP) and thrombin increased PGE ( 2 ) release from RGM1 cells for 18h, an effect being suppressed by inhibitors of COX-1, COX-2, MEK, p38 MAP kinase (p38 MAPK), protein kinase C ( PKC ), Src and EGF receptor-tyrosine kinase (EGFR-TK), but not JNK and matrix metalloproteinase ( MMP ) /a disintegrin and metalloproteinases ( ADAMs )