Enables mitogen-activated protein kinase binding activity. Involved in several processes, including positive regulation of cellular component organization; positive regulation of peptidyl-tyrosine autophosphorylation; and positive regulation of vascular associated smooth muscle cell migration. Located in growth cone. Part of protein-containing complex. Colocalizes with actin cytoskeleton; focal adhesion; and microtubule cytoskeleton. Orthologous to human IQGAP1 (IQ motif containing GTPase activating protein 1); PARTICIPATES IN E-cadherin signaling pathway; insulin responsive facilitative sugar transporter mediated glucose transport pathway; platelet-derived growth factor signaling pathway; INTERACTS WITH 1,1,1-trichloro-2,2-bis(4-hydroxyphenyl)ethane; 1-naphthyl isothiocyanate; 2,3,7,8-tetrachlorodibenzodioxine.
[NOG protein co-treated with entinostat co-treated with dorsomorphin co-treated with 4-(5-benzo(1, 3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression of IQGAP1 mRNA
[NOG protein co-treated with Panobinostat co-treated with dorsomorphin co-treated with 4-(5-benzo(1, 3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression of IQGAP1 mRNA
[NOG protein co-treated with Phenylmercuric Acetate co-treated with dorsomorphin co-treated with 4-(5-benzo(1, 3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression of IQGAP1 mRNA
[NOG protein co-treated with trichostatin A co-treated with dorsomorphin co-treated with 4-(5-benzo(1, 3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression of IQGAP1 mRNA
[NOG protein co-treated with Valproic Acid co-treated with dorsomorphin co-treated with 4-(5-benzo(1, 3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide] results in increased expression of IQGAP1 mRNA
IQGAP1 links PDGF receptor-beta signal to focal adhesions involved in vascular smooth muscle cell migration: role in neointimal formation after vascular injury.
IQGAP1, a novel vascular endothelial growth factor receptor binding protein, is involved in reactive oxygen species--dependent endothelial migration and proliferation.