マツイ　タケシ   Takeshi Matsui   松井　毅    所属   応用生物学部 応用生物学科    職種   教授
言語種別	英語
発行・発表の年月	1996
形態種別	学術論文
査読	査読あり
標題	Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho
執筆形態	共著
掲載誌名	EMBO Journal
掲載区分	国外
巻・号・頁	15(9),pp.2208-2216
総ページ数	9
著者・共著者	Takeshi Matsui, Mutsuki Amano, Takaharu Yamamoto, Kazuyasu Chihara, Masato Nakafuku, Masaaki Ito, Takeshi Nakano, Katsuya Okawa, Akihiro Iwamatsu,Kozo Kaibuchi
概要	The small GTP binding protein Rho isimplicated in cytoskeletal responses to extracellular signals such as lysophosphatidic acid to form stress fibers and focal contacts. Here we have purified a Rho-interacting protein with a molecular mass of -164 kDa (p164) from bovine brain. This protein bound to GTPγS (a non-hydrolyzable GTP analog)-RhoA but not to GDPRhoA or GTPγSRhoA with a mutation in the effector domain (RhoAA37). p164 had a kinase activity which was specificallystimulatedby GTPγS RhoA. We obtained the cDNA encoding p164 on the basis of its partial amino acid sequences and named it Rho- associated kinase (Rho-kinase). Rho-kinase has a catalytic domain in the N-terminal portion, a coiled coil domain in the middle portion and a zinc finger-like motif in the C-terminal portion. The catalytic domain shares 72% sequence homology with that of myotonic dystrophy kinase and the coiled coil domain contains a Rho-interacting interface.When COS7 cells were cotransfected with Rho-kinase and activated RhoA, some Rho-kinase was recruited to membranes. Thus it is likely that Rho-kinase is a putative target serine/ threonine kinase for Rho and serves as a mediator of the Rho-dependent signaling pathway.