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CALM1 — IQGAP1

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

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: IQGAP1 — CALM1 (physical association, affinity chromatography technology) Ren et al., J Biol Chem 2008*
• IRef Biogrid Interaction: IQGAP1 — CALM1 (direct interaction, pull down) Li et al., J Biol Chem 2003*
• IRef Biogrid Interaction: IQGAP1 — CALM1 (direct interaction, pull down) Briggs et al., J Biol Chem 2002*
• IRef Hprd Interaction: IQGAP1 — CALM1 (in vivo) Li et al., J Biol Chem 2003*, Hart et al., EMBO J 1996*
• IRef Innatedb Interaction: Complex of IQGAP1-CALM1-CTNNB1 (unknown, -) Briggs et al., J Biol Chem 2002*
• IRef Innatedb Interaction: IQGAP1 — CALM1 (unknown, -) Joyal et al., J Biol Chem 1997*
• IRef Innatedb Interaction: IQGAP1 — CALM1 (unknown, -) Li et al., J Biol Chem 2003*
• IRef Innatedb Interaction: IQGAP1 — CALM1 (unknown, -) Li et al., J Biol Chem 1999*

Text-mined interactions from Literome

Li et al., J Biol Chem 1999 : On the basis of these data, we propose that disruption of the binding of calmodulin to IQGAP1 enhances the association of IQGAP1 with components of the cadherin-catenin complex at cell-cell junctions, resulting in impaired E-cadherin function
Briggs et al., J Biol Chem 2002 : Together, our results imply that IQGAP1 enhances the function of beta-catenin in the nucleus and that calmodulin regulates this stimulation
Mateer et al., J Biol Chem 2002 : Based on this finding we hypothesized that calmodulin negatively regulates binding of IQGAP1 to F-actin
Li et al., J Biol Chem 2003 : To elucidate the molecular mechanism by which apocalmodulin and Ca ( 2+ ) /calmodulin differentially regulate IQGAP1 , a series of constructs of IQGAP1 with selected point mutations of the four tandem IQ motifs were generated
Nauert et al., J Cell Biochem 2003 : The binding of IQGAP1 to its partners is regulated by calcium/calmodulin ( Ca ( ++ ) /CaM ) and the small molecular weight guanine nucleotide triphosphatases ( GTPases ), Cdc42, and Rac1
Bashour et al., J Cell Biol 1997 : Exogenous calmodulin partially inhibited binding of IQGAP1 to F-actin, and was more effective in the absence, than in the presence of calcium ... These results, in conjunction with prior evidence that IQGAP1 binds directly to activated Rac and Cdc42, suggest that IQGAP1 serves as a direct molecular link between these GTPases and the actin cytoskeleton, and that the actin binding activity of IQGAP1 is regulated by calmodulin