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BAIAP2 — RAC1

Pathways - manually collected, often from reviews:

• KEGG Adherens junction: RAC1/RAC2/RAC3 → Complex of BAIAP2-WASF1-WASF2-WASF3 (protein-protein, activation)
  
• KEGG Regulation of actin cytoskeleton: RAC1/RAC2/RAC3 → BAIAP2 (protein-protein, activation)
• NCI Pathway Database RAC1 signaling pathway: RAC1/GTP complex (RAC1) → IRSP53 (BAIAP2) (modification, activates) Steffen et al., EMBO J 2004*, Suetsugu et al., J Cell Biol 2006, Yamazaki et al., J Cell Sci 2007, Abou-Kheir et al., J Cell Sci 2008*, Ryu et al., Mol Cell Biol 2009, Ismail et al., Nature structural & molecular biology 2009
  Evidence: assay, physical interaction
• NCI Pathway Database ErbB1 downstream signaling: RAC1/GTP complex (RAC1) → IRSP53 (BAIAP2) (modification, activates) Innocenti et al., J Cell Biol 2002, Eden et al., Nature 2002, Steffen et al., EMBO J 2004*, Sini et al., Nat Cell Biol 2004, Innocenti et al., Nat Cell Biol 2004
  Evidence: mutant phenotype
• NCI Pathway Database PDGFR-beta signaling pathway: RAC1/GTP complex (RAC1) → IRSP53 (BAIAP2) (modification, activates) Innocenti et al., J Cell Biol 2002, Eden et al., Nature 2002, Steffen et al., EMBO J 2004*, Sini et al., Nat Cell Biol 2004, Innocenti et al., Nat Cell Biol 2004, Leng et al., Proc Natl Acad Sci U S A 2005
  Evidence: assay, physical interaction
• Reactome Reaction: RAC1 → BAIAP2 (reaction) Suetsugu et al., J Cell Biol 2006, Miki et al., EMBO J 1998
• Reactome Reaction: RAC1 → BAIAP2 (indirect_complex) Leng et al., Proc Natl Acad Sci U S A 2005, Suetsugu et al., J Cell Biol 2006, Nakanishi et al., J Biochem 2007, Mendoza et al., Mol Cell 2011, Miki et al., EMBO J 1998
• WikiPathways Regulation of Actin Cytoskeleton: RAC1/RAC3/RAC2 → BAIAP2 (activation)

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: RAC1 — BAIAP2 (physical association, affinity chromatography technology) Govind et al., J Cell Biol 2001*
• IRef Biogrid Interaction: RAC1 — BAIAP2 (direct interaction, pull down) Miki et al., Nature 2000*
• IRef Hprd Interaction: BAIAP2 — RAC1 (in vitro) Miki et al., Nature 2000*, Miki et al., Biochem Biophys Res Commun 2002*, Roy et al., J Cell Biol 2009*
• IRef Hprd Interaction: BAIAP2 — RAC1 (in vivo) Miki et al., Nature 2000*, Miki et al., Biochem Biophys Res Commun 2002*, Roy et al., J Cell Biol 2009*
• IRef Intact Interaction: RAC1 — BAIAP2 (physical association, two hybrid) Krugmann et al., Curr Biol 2001*
• IRef Intact Interaction: RAC1 — BAIAP2 (physical association, pull down) Suetsugu et al., J Biol Chem 2006*
• IRef Intact Interaction: RAC1 — BAIAP2 (physical association, biosensor) Suetsugu et al., J Biol Chem 2006*
• IRef Intact Interaction: BAIAP2 — RAC1 (physical association, pull down) Roy et al., J Cell Biol 2009*
• IRef Intact Interaction: Complex of BAIAP2-KANK1-RAC1 (association, anti bait coimmunoprecipitation) Roy et al., J Cell Biol 2009*

Text-mined interactions from Literome

Miki et al., Nature 2000 : From studies of ectopic expression, we found that IRSp53 is essential for Rac to induce membrane ruffling, probably because it recruits WAVE, which stimulates actin polymerization mediated by the Arp2/3 complex
Suetsugu et al., J Cell Biol 2006 : Purified WAVE2 and purified WAVE2 complex were activated by IRSp53 in a Rac dependent manner with PIP ( 3 ) -containing liposomes
Abou-Kheir et al., J Cell Sci 2008 : Membrane targeting of WAVE2 is not sufficient for WAVE2 dependent actin polymerization : a role for IRSp53 in mediating the interaction between Rac and WAVE2 ... Importantly, reduction of endogenous IRSp53 or expression of IRSp53 lacking the WAVE2 binding site ( IRSp53DeltaSH3 ) resulted in a significant reduction in the association of Rac1 with WAVE2 and Abi1, indicating that the association of Rac1 with WAVE2 and Abi1 is IRSp53 dependent
Teodorof et al., Exp Cell Res 2009 : SPIN90 and IRSp53 positively cooperated to mediate Rac activation, and co-expression of SPIN90 and IRSp53 in COS-7 cells led to the complex formation of SPIN90-IRSp53 in the leading edge of cells