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Titolo:
THE SMALL GTP-BINDING PROTEIN RHO BINDS TO AND ACTIVATES A 160-KDA SER THR PROTEIN-KINASE HOMOLOGOUS TO MYOTONIC-DYSTROPHY KINASE/
Autore:
ISHIZAKI T; MAEKAWA M; FUJISAWA K; OKAWA K; IWAMATSU A; FUJITA A; WATANABE N; SAITO Y; KAKIZUKA A; MORII N; NARUMIYA S;
Indirizzi:
KYOTO UNIV,FAC MED,DEPT PHARMACOL KYOTO 606 JAPAN KYOTO UNIV,FAC MED,DEPT PHARMACOL KYOTO 606 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA 236 JAPAN
Titolo Testata:
EMBO journal
fascicolo: 8, volume: 15, anno: 1996,
pagine: 1885 - 1893
SICI:
0261-4189(1996)15:8<1885:TSGPRB>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
SWISS 3T3 CELLS; ADP-RIBOSYLATION; GENE-PRODUCT; RIBOSYLTRANSFERASE; AGGREGATION; RECEPTOR; DIVISION; REQUIRES; DOMAINS; FAMILY;
Keywords:
COILED-COIL STRUCTURE; MYOTONIC DYSTROPHY KINASE; PROTEIN KINASE; RHO; SMALL GTP-BINDING PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
62
Recensione:
Indirizzi per estratti:
Citazione:
T. Ishizaki et al., "THE SMALL GTP-BINDING PROTEIN RHO BINDS TO AND ACTIVATES A 160-KDA SER THR PROTEIN-KINASE HOMOLOGOUS TO MYOTONIC-DYSTROPHY KINASE/", EMBO journal, 15(8), 1996, pp. 1885-1893

Abstract

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 similar to 600 amino acids long, and a cysteine-rich zinc fingerlike 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 01:59:37