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The Pyst2-L phosphatase is involved in cell-crowding.
Levy-Nissenbaum, Orlev; Ben-Menachem, Shlomit; Sagi-Assif, Orit; Witz, Isaac P.
Afiliação
  • Levy-Nissenbaum O; Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel-Aviv University, 69978 Tel Aviv, Israel. orle@post.tau.ac.il
Immunol Lett ; 104(1-2): 138-45, 2006 Apr 15.
Article em En | MEDLINE | ID: mdl-16386315
ABSTRACT
The dual-specificity phosphatase Pyst2-L was found to be over expressed in leukocytes derived from AML and ALL patients as well as in certain other solid tumors and lymphoblastoid cell lines. Pyst2-L, binds and dephosphorylates both pERKs and pJNKs proteins, and thus, plays a role in regulating the MAP kinase signaling pathway. In the present study, a comparative genomic application was used and sequence analysis of multi-organisms databases were searched in order to identify genes homologous to Pyst2-L. The Xenopus laevis MAP kinase phosphatase X17c gene and the Yeast nitrogen starvation-induced protein phosphatase Yvh1p gene were revealed to be highly homologous with Pyst2-L. Both X17c and Yvh1p genes play a role in cell cycle regulation. A down regulated expression of the Yvh1p gene occurred in Saccharomyces cerevisiae that were synchronized to the G2-phase of the cell cycle by alpha-factor. In conformity with this result, a reduction in Pyst2-L expression levels was observed in G2-phase-synchronized Human K562 cells. Finally, we were able to show that cells in highly crowded cultures express high levels of the Pyst2-L phosphatase. These observations may indicate that low levels of the Pyst2-L phosphatase are essential for the G2-phase of the cell cycle and that this phosphatase might play a role in signaling cascades induced by cellular crowding.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ciclo Celular / Proteínas Tirosina Fosfatases / Fosfoproteínas Fosfatases / Proteínas de Xenopus / Proteínas de Saccharomyces cerevisiae Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: Immunol Lett Ano de publicação: 2006 Tipo de documento: Article País de afiliação: Israel
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ciclo Celular / Proteínas Tirosina Fosfatases / Fosfoproteínas Fosfatases / Proteínas de Xenopus / Proteínas de Saccharomyces cerevisiae Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: Immunol Lett Ano de publicação: 2006 Tipo de documento: Article País de afiliação: Israel