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      A brain serine/threonine protein kinase activated by Cdc42 and Rac1.

      Nature
      Amino Acid Sequence, Animals, Brain, enzymology, Cattle, Enzyme Activation, GTP Phosphohydrolases, antagonists & inhibitors, GTP-Binding Proteins, metabolism, Guanosine Diphosphate, Guanosine Triphosphate, Intracellular Signaling Peptides and Proteins, MAP Kinase Kinase Kinases, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Rats, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Signal Transduction, p21-Activated Kinases, rac GTP-Binding Proteins, rho GTP-Binding Proteins

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          Abstract

          A new brain serine/threonine protein kinase may be a target for the p21ras-related proteins Cdc42 and Rac1. The kinase sequence is related to that of the yeast protein STE20, implicated in pheromone-response pathways. The kinase complexes specifically with activated (GTP-bound) p21, inhibiting p21 GTPase activity and leading to kinase autophosphorylation and activation. Autophosphorylated kinase has a decreased affinity for Cdc42/Rac, freeing the p21 for further stimulatory activities or downregulation by GTPase-activating proteins. This bimolecular interaction provides a model for studying p21 regulation of mammalian phosphorylation signalling pathways.

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