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*
Department of Immunology and Oncology, Centro Nacional de Biotecnología, Campus de Cantoblanco, Madrid, Spain;
Laboratoire de Physiologie de la Reproduction, Equipe Scientifique Associé Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, and
Département d’Immunologie, Laboratoire de Signalisation Immunoparasitaire, Institut Pasteur, Paris, France
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-
-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.
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