@misc{10481/100804,
year = {2001},
url = {https://hdl.handle.net/10481/100804},
abstract = {The diverse forms of protein phosphatase 1 (PP1) in vivo result from the association of the catalytic subunit with different regulatory subunits. We recently have described that PP1alpha is a Ras-activated Bad phosphatase that regulates IL-2 deprivation-induced apoptosis. With the yeast two-hybrid system, GST fusion proteins, indirect immunofluorescence, and coimmunoprecipitation, we found that Bcl-2 interacts with PP1alpha and Bad. In contrast, Bad did not interact with 14-3-3 protein. Bcl-2 depletion decreased phosphatase activity and association of PP1alpha to Bad. Bcl-2 contains the RIVAF motif, analogous to the well characterized R/KXV/IXF consensus motif shared by most PP1-interacting proteins. This sequence is involved in the binding of Bcl-2 to PP1alpha. Disruption of Bcl-2/PP1alpha association strongly decreased Bcl-2 and Bad-associated phosphatase activity and formation of the trimolecular complex. These results suggest that Bcl-2 targets PP1alpha to Bad.},
publisher = {The American Association of Immunologists, Inc.},
title = {Bcl-2 Targets Protein Phosphatase 1α to Bad},
doi = {10.4049/jimmunol.166.12.7345},
author = {Ayllón, Verónica and Cayla, Xavier and García, Alphonse and Roncal, Francisco and Albar, Juan Pablo and Martínez-A, Carlos and Rebollo, Angelita},
}