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Pleckstrin homology domain interacts with Rkp1/Cpc2, a RACK1 homolog, to modulate Pck2-mediated signaling process in Schizosaccharomyces pombe.
Won, M; Jang, Y J; Chung, K S; Kim, D U; Hoe, K L; Han, M Y; Kim, H B; Lee, S H; Oh, H W; Yoo, H S.
Afiliación
  • Won M; Genome Research Center, Korea Research Institute of Biotechnology and Bioscience, Taejon, 305-600, Korea. misun@mail.kribb.re.kr
Biochem Biophys Res Commun ; 289(5): 987-92, 2001 Dec 21.
Article en En | MEDLINE | ID: mdl-11741288
Rkp1/Cpc2, a fission yeast RACK1 homolog, interacts with Pck2, a PKC homolog, and is involved in the regulation of pck2-mediated signaling process. The N-terminal region of split pleckstrin homology domain (nPH) in human PLC-gamma1 bound to Rkp1/Cpc2 concomitantly with Pck2. nPH inhibited kinase activity of GST-Pck2 purified from Schizosaccharomyces pombe in vitro. The lethality induced by pck2(+) overexpression was suppressed by coexpression of either rkp1(+) or nPH domain. This result suggests that Rkp1/Cpc2 interacts with PH domain-containing protein and regulates the Pck2-mediated signaling process in S. pombe.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfoproteínas / Schizosaccharomyces / Proteínas Sanguíneas / Receptores de Superficie Celular / Proteínas de Neoplasias Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2001 Tipo del documento: Article Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfoproteínas / Schizosaccharomyces / Proteínas Sanguíneas / Receptores de Superficie Celular / Proteínas de Neoplasias Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2001 Tipo del documento: Article Pais de publicación: Estados Unidos