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Titolo:
RHO-ASSOCIATED KINASE, A NOVEL SERINE THREONINE KINASE, AS A PUTATIVETARGET FOR THE SMALL GTP-BINDING PROTEIN-RHO
Autore:
MATSUI T; AMANO M; YAMAMOTO T; CHIHARA K; NAKAFUKU M; ITO M; NAKANO T; OKAWA K; IWAMATSU A; KAIBUCHI K;
Indirizzi:
NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT,8916-5 TAKAYAMA NARA 63001 JAPAN NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT NARA 63001 JAPAN MIE UNIV,SCH MED,DEPT INTERNAL MED 1 TSU MIE 514 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN
Titolo Testata:
EMBO journal
fascicolo: 9, volume: 15, anno: 1996,
pagine: 2208 - 2216
SICI:
0261-4189(1996)15:9<2208:RKANST>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-CLONING; EXCHANGE PROTEIN; MYOTONIC-DYSTROPHY; ADP-RIBOSYLATION; NADPH OXIDASE; CTG REPEAT; GENE; ACTIVATION; SEQUENCES; GDI;
Keywords:
CYTOSKELETON; GTP BINDING PROTEIN; PHOSPHORYLATION; PROTEIN KINASE; RHO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
59
Recensione:
Indirizzi per estratti:
Citazione:
T. Matsui et al., "RHO-ASSOCIATED KINASE, A NOVEL SERINE THREONINE KINASE, AS A PUTATIVETARGET FOR THE SMALL GTP-BINDING PROTEIN-RHO", EMBO journal, 15(9), 1996, pp. 2208-2216

Abstract

The small GTP binding protein Rho is implicated 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 similar to 164 kDa (p164) from bovine brain. This protein bound to GTP gamma S (a non-hydrolyzable GTP analog). RhoA but not to GDP . RhoA or GTP gamma S . RhoA with a mutation in the effector domain (Rho(A37)). p164 had a kinase activity which was specifically stimulated by GTP gamma S . 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 catalyticdomain in the N-terminal portion, a coiled coil domain in the middle portion and a zinc finger-like moth 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 03:12:51