Your browser doesn't support javascript.
loading
Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase.
Koyama, M; Ito, M; Feng, J; Seko, T; Shiraki, K; Takase, K; Hartshorne, D J; Nakano, T.
Afiliación
  • Koyama M; First Department of Internal Medicine, Mie University School of Medicine, Tsu, Mie 514-8507, Japan.
FEBS Lett ; 475(3): 197-200, 2000 Jun 23.
Article en En | MEDLINE | ID: mdl-10869555
Phosphorylation of CPI-17 by Rho-associated kinase (Rho-kinase) and its effect on myosin phosphatase (MP) activity were investigated. CPI-17 was phosphorylated by Rho-kinase to 0.92 mol of P/mol of CPI-17 in vitro. The inhibitory phosphorylation site was Thr(38) (as reported previously) and was identified using a point mutant of CPI-17 and a phosphorylation state-specific antibody. Phosphorylation by Rho-kinase dramatically increased the inhibitory effect of CPI-17 on MP activity. Thus, CPI-17 as a substrate of Rho-kinase could be involved in the Ca(2+) sensitization of smooth muscle contraction as a downstream effector of Rho-kinase.
Asunto(s)
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfoproteínas / Proteínas Serina-Treonina Quinasas / Fosfoproteínas Fosfatasas / Proteínas Musculares / Músculo Liso Límite: Animals Idioma: En Revista: FEBS Lett Año: 2000 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfoproteínas / Proteínas Serina-Treonina Quinasas / Fosfoproteínas Fosfatasas / Proteínas Musculares / Músculo Liso Límite: Animals Idioma: En Revista: FEBS Lett Año: 2000 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido