PMID:12115603

Citation	Ayllón, V, Cayla, X, García, A, Fleischer, A and Rebollo, A (2002) The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad. Eur. J. Immunol. 32:1847-55
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.
Links	PubMed Online version:<1847::AID-IMMU1847>3.0.CO;2-7 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7
Keywords	Animals; Apoptosis; Apoptosis Regulatory Proteins; Binding Sites; Carrier Proteins/metabolism; Cell Line; Enzyme Inhibitors/pharmacology; HeLa Cells; Humans; Mice; Okadaic Acid/pharmacology; Phosphoprotein Phosphatases/antagonists & inhibitors; Phosphoprotein Phosphatases/metabolism; Protein Phosphatase 1; Proteins/metabolism; Proto-Oncogene Proteins c-bcl-2/metabolism; bcl-Associated Death Protein; bcl-X Protein
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