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http://purl.uniprot.org/citations/8617235http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8617235http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8617235http://www.w3.org/2000/01/rdf-schema#comment"The small GTP-binding protein Rho functions as a molecular switch in the formation of focal adhesions and stress fibers, cytokinesis and transcriptional activation. The biochemical mechanism underlying these actions remains unknown. Using a ligand overlay assay, we purified a 160 kDa platelet protein that bound specifically to GTP-bound Rho. This protein, p160, underwent autophosphorylation at its serine and threonine residues and showed the kinase activity to exogenous substrates. Both activities were enhanced by the addition of GTP-bound Rho. A cDNA encoding p160 coded for a 1354 amino acid protein. This protein has a Ser/Thr kinase domain in its N-terminus, followed by a coiled-coil structure approximately 600 amino acids long, and a cysteine-rich zinc finger-like motif and a pleckstrin homology region in the C-terminus. The N-terminus region including a kinase domain and a part of coiled-coil structure showed strong homology to myotonic dystrophy kinase over 500 residues. When co-expressed with RhoA in COS cells, p160 was co-precipitated with the expressed Rho and its kinase activity was activated, indicating that p160 can associate physically and functionally with Rho both in vitro and in vivo."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1996.tb00539.x"xsd:string
http://purl.uniprot.org/citations/8617235http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1996.tb00539.x"xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Iwamatsu A."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Iwamatsu A."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Maekawa M."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Maekawa M."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Narumiya S."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Narumiya S."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Watanabe N."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Watanabe N."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Fujita A."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Fujita A."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Fujisawa K."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Fujisawa K."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Kakizuka A."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Kakizuka A."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Okawa K."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Okawa K."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Ishizaki T."xsd:string
http://purl.uniprot.org/citations/8617235http://purl.uniprot.org/core/author"Ishizaki T."xsd:string