@misc{10481/100812,
year = {2002},
url = {https://hdl.handle.net/10481/100812},
abstract = {Many molecules relocate subcellularly in cells undergoing apoptosis. Using coimmunoprecipitation experiments we demonstrate that Bad is not associated to 14-3-3 protein, suggesting a new mechanism for the control of the proapoptotic role of Bad. Here we show, by confocal microscopy and cellular fractionation, that Bad is attached to lipid rafts in IL-4-stimulated cells and thymocytes while associated with mitochondria in IL-4-deprived cells. Disruption of lipid rafts by methyl-beta-cyclodextrin treatment induces segregation of Bad from rafts, which correlates with apoptosis. Our results suggest that the interaction of Bad with rafts is a dynamic process regulated by IL-4 and involved in the control of apoptosis.},
organization = {Department of Immunology and Oncology, Centro Nacional de Biotecnología, Campus de Cantoblanco, Madrid, Spain},
publisher = {The American Association of Immunologists, Inc.},
title = {Segregation of bad from lipid rafts is implicated in the induction of apoptosis},
doi = {10.4049/jimmunol.168.7.3387},
author = {Ayllón Cases, Verónica and Fleischer, Aarne and Cayla, Xavier and García, Alphonse and Rebollo, Angelita},
}