Segregation of Bad from lipid rafts is implicated in the induction of apoptosis.
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.
Ayllón
Verónica
V
Department of Immunology and Oncology, Centro Nacional de Biotecnología, Campus de Cantoblanco, Madrid, Spain.
Fleischer
Aarne
A
Cayla
Xavier
X
García
Alphonse
A
Rebollo
Angelita
A
D000818:Animals; D017209:Apoptosis / Q000276:immunology*; D015153:Blotting, Western; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000502:physiology; D002460:Cell Line; D002470:Cell Survival / Q000276:immunology; D015847:Interleukin-4 / Q000494:pharmacology; D021962:Membrane Microdomains / Q000378:metabolism* / Q000502:physiology; D051379:Mice; D008928:Mitochondria / Q000378:metabolism; D051025:bcl-Associated Death Protein
C494820:Bad protein, mouse; D002352:Carrier Proteins; D051025:bcl-Associated Death Protein; D015847:Interleukin-4