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KDR — PLCG1

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: PLCG1 → KDR (increases, KDR Activity, PLCG1 Activity) Soldi et al., EMBO J 1999
  Evidence: Through its phosphorylated tyrosine residues, the activated VEGFR-2 associates with the adapter molecules Shc, Grb2 and Nck, to Ras GTPase activating protein, p59fyn, pp62yes and phospholipase Cg, and to the tyrosine phosphatases SHP-1 and SHP-2
• OpenBEL Selventa BEL large corpus: PLCG1 → KDR (directlyIncreases, PLCG1 Activity)
  Evidence: 96108162;1689310;1708307
• KEGG VEGF signaling pathway: KDR → PLCG1/PLCG2 (protein-protein, activation)
• NCI Pathway Database Signaling events mediated by VEGFR1 and VEGFR2: VEGFR1/2 (dimer)/VEGFA (dimer) complex (VEGFA-FLT1-KDR) → PLCgamma1 (PLCG1) (modification, activates) Huang et al., Int J Biochem Cell Biol 2001*, Cunningham et al., Biochem Biophys Res Commun 1997
  Evidence: assay, physical interaction
• Reactome Reaction: PLCG1 → KDR (reaction) Takahashi et al., EMBO J 2001*, McLaughlin et al., Am J Physiol Cell Physiol 2001*
• Reactome Reaction: PLCG1 → KDR (indirect_complex) Takahashi et al., EMBO J 2001*, McLaughlin et al., Am J Physiol Cell Physiol 2001*, Serrano et al., J Immunol 2005, Gresset et al., J Biol Chem 2010*
• WikiPathways Angiogenesis: FLT1/FGFR2/TEK/KDR → SMAD1/PIK3CA/SRC/PTK2/MAPK14/PLCG1 (activation)
  

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: KDR — PLCG1 Matthews et al., Eur J Biochem 2000*
• IRef Bind_translation Interaction: KDR — PLCG1 (unspecified method) Matthews et al., Eur J Biochem 2000*
• IRef Biogrid Interaction: KDR — PLCG1 (direct interaction, pull down) Cunningham et al., Biochem Biophys Res Commun 1997
• IRef Hprd Interaction: KDR — PLCG1 (in vivo) Meyer et al., J Biol Chem 2003*
• IRef Hprd Interaction: KDR — PLCG1 (in vitro) Meyer et al., J Biol Chem 2003*
• IRef Intact Interaction: KDR — PLCG1 (association, pull down) Meyer et al., J Biol Chem 2003*
• IRef Mppi Interaction: KDR — PLCG1 (two hybrid) Matthews et al., Eur J Biochem 2000*
• IRef Mppi Interaction: KDR — PLCG1 (coimmunoprecipitation) Matthews et al., Eur J Biochem 2000*

Text-mined interactions from Literome

Wu et al., J Biol Chem 2000 : Two-hybrid cloning and immunoprecipitation from human umbilical vein endothelial cells ( HUVEC ) showed that KDR binds to and promotes the tyrosine phosphorylation of phospholipase Cgamma ( PLCgamma )
Gille et al., J Biol Chem 2001 : KDR stimulation caused tyrosine phosphorylation of both phosphatidylinositol 3-kinase and phospholipase Cgamma in primary endothelial cells and stimulated cell migration
Meyer et al., J Biol Chem 2003 : Mutation of tyrosines 799, 820, 949, 994, 1080, 1173, and 1221 had no measurable effect on the ability of VEGFR-2 to stimulate PLCgamma1 activation ... Taken together, the results indicate that phosphorylation of tyrosine 1006 is essential for VEGFR-2 mediated PLCgamma1 activation, calcium flux, and cell differentiation
Singh et al., Proc Natl Acad Sci U S A 2007 : A critical role for the E3-ligase activity of c-Cbl in VEGFR-2 mediated PLCgamma1 activation and angiogenesis