期刊
NATURE CELL BIOLOGY
卷 5, 期 12, 页码 1051-1061出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1063
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- NIDA NIH HHS [DA-000266, DA-00074] Funding Source: Medline
- NIH HHS [NH65090] Funding Source: Medline
- NIMH NIH HHS [MH-18501] Funding Source: Medline
- NINDS NIH HHS [NS-043850] Funding Source: Medline
Mitochondrial cytochrome c release and inositol (1,4,5) trisphosphate receptor (InsP(3)R)-mediated calcium release from the endoplasmic reticulum mediate apoptosis in response to specific stimuli. Here we show that cytochrome c binds to the InsP(3)R during apoptosis. Addition of 1 nM cytochrome c blocks calcium-dependent inhibition of InsP(3)R function. Early in apoptosis, cytochrome c translocates to the endoplasmic reticulum where it selectively binds InsP(3)R, resulting in sustained, oscillatory cytosolic calcium increases. These calcium events are linked to the coordinate release of cytochrome c from all mitochondria. Our findings identify a feed-forward mechanism whereby early cytochrome c release increases InsP(3)R function, resulting in augmented cytochrome c release that amplifies the apoptotic signal.
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