کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1939811 | 1050767 | 2006 | 6 صفحه PDF | دانلود رایگان |
Glycogen synthase kinase (GSK)-3β has emerged as a key molecule that regulates neuronal apoptosis. To examine the molecular mechanism(s) through which GSK-3β regulates this process, we studied the subcellular localization of GSK-3β following exposure of the cells to well-characterized apoptotic stimuli. Here, we report that the induction of apoptosis by withdrawal of serum and potassium triggers dephosphorylation of GSK-3β at serine 9 and subsequent translocation of these molecules into neuronal lipid raft microdomains. Inhibition of GSK-3β by small molecule inhibitors blocks specific phosphorylation of lipid raft associated protein Tau. Consistent with the notion that the lipid raft domains may serve as a platform for the cellular signaling complexes, disruption of lipid rafts protected neurons from apoptosis induced by withdrawal of serum and potassium as well as by HIV-1 Tat. Our observations reveal novel interaction of GSK-3β and raft domains, and suggest that such interaction could contribute to neuronal apoptosis.
Journal: Biochemical and Biophysical Research Communications - Volume 345, Issue 4, 14 July 2006, Pages 1643–1648