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Título: | Attenuation of ribosomal protein S6 phosphatase activity in chicken embryo fibroblasts transformed by Rous sarcoma virus |
Autor: | Belandia, Borja CSIC ORCID; Brautigan, D.; Martín-Pérez, Jorge CSIC ORCID | Fecha de publicación: | 1994 | Editor: | American Society for Microbiology | Citación: | Molecular and Cellular Biology 14(1): 200-206 (1994) | Resumen: | In chicken embryo fibroblasts, phosphorylation of the 40S ribosomal protein S6 increases during G1 but returns to basal level by mitosis. In contrast, in Rous sarcoma virus (RSV)-transformed fibroblasts, S6 remains highly phosphorylated throughout mitosis. This study investigated the mechanism by which RSV alters the pattern of S6 phosphorylation. Pulse-chase experiments demonstrate that phosphate turnover in S6 is rapid in normal cells and in cells infected with an RSV transformation-defective virus. In contrast, phosphate turnover in S6 is severely reduced in cells infected with temperature-sensitive RSV at a temperature permissive for transformation, indicating a diminished S6 phosphatase activity. Fractionation of cell lysates by DEAE chromatography showed an almost threefold lower S6 phosphatase activity in RSV-transformed versus normal cells. The S6 phosphatase was sensitive to inhibitor 2 and specifically recognized by an antibody to type 1 phosphatase (PP1). The S6 phosphatase activity recovered by immunoprecipitation of PP1 was threefold lower in transformed cells, but the steady-state level of expression and the rate of synthesis of PP1 were not altered by oncogenic transformation. Together, the results show that transformation by RSV reduced the S6-PP1 activity. | Versión del editor: | http://mcb.asm.org/content/14/1/200.short | URI: | http://hdl.handle.net/10261/78904 | DOI: | 10.1128/MCB.14.1.200 | Identificadores: | doi: 10.1128/MCB.14.1.200 issn: 0270-7306 e-issn: 1098-5549 |
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