The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1α to Bad Ayllón, Verónica Cayla, Xavier García, Alphonse Fleischer, Aarne Rebollo, Angelita Centro Nacional de Biotenología, Department of Immunology and Oncology, Campus de Cantoblanco, UAM, Madrid, Spain Laboratoire d'Immunologie Cellulaire et Tissulaire, INSERM U543, Bâtiment CERVI, Hôpital Pitié Salpêtrière, Paris, France Bcl-xL and Bcl-w specifically interact with PP1α 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)α 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 PP1α. Disruption of Bcl-xL/PP1α or Bcl-w/PP1α association strongly decreases Bad-associated phosphataseactivity and stability of trimolecular complexes. These results suggest that Bcl-xL and Bcl-w are PP1α targeting subunits and this trimolecular complex may be involved in the control of apoptosis. 2025-01-28T13:43:04Z 2025-01-28T13:43:04Z 2002 journal article V. Ayllón et al. The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1α to Bad. Eur. J. Immunol. 2002. 32: 1847–1855. https://doi.org/10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7 https://hdl.handle.net/10481/100830 10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7 eng http://creativecommons.org/licenses/by-nc-nd/4.0/ open access Attribution-NonCommercial-NoDerivatives 4.0 Internacional Wiley