Segregation of bad from lipid rafts is implicated in the induction of apoptosis

被引：39

作者：

Ayllón, V

Fleischer, A

Cayla, X

García, A

Rebollo, A

机构：

[1] Univ Autonoma Madrid, Ctr Nacl Biotecnol, Dept Immunol & Oncol, E-28049 Madrid, Spain

[2] CNRS, ESA, INRA, Reprod Physiol Lab, Paris, France

[3] Inst Pasteur, Dept Immunol, Lab Signalisat Immunoparasitaire, Paris, France

来源：

JOURNAL OF IMMUNOLOGY | 2002年 / 168卷 / 07期

关键词：

D O I：

10.4049/jimmunol.168.7.3387

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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.

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页码：3387 / 3393

页数：7

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