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• W2057843984 abstract "Bcl-xL and Bcl-w specifically interact with PP1alpha and Bad. A phosphatase activity sensitive to okadaic acid was detected in Bcl-xL, Bcl-w and Bad immunoprecipitates. Serine phosphorylation of Bcl-xL and Bcl-w correlates with the number of trimolecular complexes formed. Depletion of Bcl-xL and Bcl-w decreases the remaining Bad-associated phosphatase activity and association of protein phosphatase 1 (PP1)alpha to Bad. Bcl-xL and Bcl-w contain the R/K X V/I X F consensus motif shared by PP1 targeting subunits. This motif, in addition to F X X R X R motif, is involved in binding of Bcl-xL and Bcl-w to PP1alpha. Disruption of Bcl-xL/PP1alpha or Bcl-w/PP1alpha association strongly decreases Bad-associated phosphataseactivity and stability of trimolecular complexes. These results suggest that Bcl-xL and Bcl-w are PP1alpha targeting subunits and this trimolecular complex may be involved in the control of apoptosis." @default.
• W2057843984 created "2016-06-24" @default.
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• W2057843984 date "2002-07-01" @default.
• W2057843984 modified "2023-10-17" @default.
• W2057843984 title "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1α to Bad" @default.
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• W2057843984 doi "https://doi.org/10.1002/1521-4141(200207)32:7<1847::aid-immu1847>3.0.co;2-7" @default.
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