| pubmed-article:12668660 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1424489 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0230871 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1999177 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:12668660 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:12668660 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:12668660 | pubmed:dateCreated | 2003-4-1 | lld:pubmed |
| pubmed-article:12668660 | pubmed:abstractText | Stimulation of cell surface death receptors activates caspase-8, which targets a limited number of substrates including BAP31, an integral membrane protein of the endoplasmic reticulum (ER). Recently, we reported that a caspase-resistant BAP31 mutant inhibited several features of Fas-induced apoptosis, including the release of cytochrome c (cyt.c) from mitochondria (Nguyen, M., D.G. Breckenridge, A. Ducret, and G.C. Shore. 2000. Mol. Cell. Biol. 20:6731-6740), implicating ER-mitochondria crosstalk in this pathway. Here, we report that the p20 caspase cleavage fragment of BAP31 can direct pro-apoptotic signals between the ER and mitochondria. Adenoviral expression of p20 caused an early release of Ca2+ from the ER, concomitant uptake of Ca2+ into mitochondria, and mitochondrial recruitment of Drp1, a dynamin-related protein that mediates scission of the outer mitochondrial membrane, resulting in dramatic fragmentation and fission of the mitochondrial network. Inhibition of Drp1 or ER-mitochondrial Ca2+ signaling prevented p20-induced fission of mitochondria. p20 strongly sensitized mitochondria to caspase-8-induced cyt.c release, whereas prolonged expression of p20 on its own ultimately induced caspase activation and apoptosis through the mitochondrial apoptosome stress pathway. Therefore, caspase-8 cleavage of BAP31 at the ER stimulates Ca2+-dependent mitochondrial fission, enhancing the release of cyt.c in response to this initiator caspase. | lld:pubmed |
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| pubmed-article:12668660 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12668660 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12668660 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12668660 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:12668660 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:12668660 | pubmed:author | pubmed-author:ShoreGordon... | lld:pubmed |
| pubmed-article:12668660 | pubmed:author | pubmed-author:BreckenridgeD... | lld:pubmed |
| pubmed-article:12668660 | pubmed:author | pubmed-author:MarcellusRich... | lld:pubmed |
| pubmed-article:12668660 | pubmed:author | pubmed-author:StojanovicMar... | lld:pubmed |
