RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate receptor signaling.
Cadherin adhesion molecules are believed to be important for synaptic plasticity. beta-Catenin, which links cadherins and the actin cytoskeleton, is a modulator of cadherin adhesion and regulates synaptic structure and function. Here we show that beta-catenin interacts with a novel GTPase-activating protein, named RICS, that acts on Cdc42 and Rac1. ... The RICS-beta-catenin complex was found to be associated with N-cadherin, N-methyl-d-aspartate receptors, and postsynaptic density-95, and localized to the postsynaptic density. Furthermore, the GTPase-activating protein activity of RICS was inhibited by phosphorylation by Ca(2+)/calmodulin-dependent protein kinase II. These results suggest that RICS is involved in the synaptic adhesion- and N-methyl-d-aspartate-mediated organization of cytoskeletal networks and signal transduction. Thus, RICS may regulate dendritic spine morphology and strength by modulating Rho GTPases.
Mesh Terms:
Amino Acid Sequence, Animals, Blotting, Northern, Brain, Cadherins, Calcium, Cells, Cultured, Cloning, Molecular, Cytoskeletal Proteins, Cytoskeleton, DNA, Complementary, Dose-Response Relationship, Drug, Down-Regulation, Enzyme Activation, GTP Phosphohydrolases, GTPase-Activating Proteins, Hippocampus, Humans, Immunoblotting, Mice, Molecular Sequence Data, N-Methylaspartate, Nerve Tissue Proteins, Neurons, Phosphoric Monoester Hydrolases, Phosphorylation, Plasmids, Precipitin Tests, Protein Structure, Tertiary, RNA, Messenger, Rats, Sequence Homology, Amino Acid, Signal Transduction, Subcellular Fractions, Time Factors, Trans-Activators, Two-Hybrid System Techniques, beta Catenin, cdc42 GTP-Binding Protein, rac1 GTP-Binding Protein, rho GTP-Binding Proteins
Amino Acid Sequence, Animals, Blotting, Northern, Brain, Cadherins, Calcium, Cells, Cultured, Cloning, Molecular, Cytoskeletal Proteins, Cytoskeleton, DNA, Complementary, Dose-Response Relationship, Drug, Down-Regulation, Enzyme Activation, GTP Phosphohydrolases, GTPase-Activating Proteins, Hippocampus, Humans, Immunoblotting, Mice, Molecular Sequence Data, N-Methylaspartate, Nerve Tissue Proteins, Neurons, Phosphoric Monoester Hydrolases, Phosphorylation, Plasmids, Precipitin Tests, Protein Structure, Tertiary, RNA, Messenger, Rats, Sequence Homology, Amino Acid, Signal Transduction, Subcellular Fractions, Time Factors, Trans-Activators, Two-Hybrid System Techniques, beta Catenin, cdc42 GTP-Binding Protein, rac1 GTP-Binding Protein, rho GTP-Binding Proteins
J. Biol. Chem.
Date: Mar. 14, 2003
PubMed ID: 12531901
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