| pubmed-article:17535899 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0234402 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:17535899 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:17535899 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:17535899 | pubmed:dateCreated | 2007-6-13 | lld:pubmed |
| pubmed-article:17535899 | pubmed:abstractText | The multidomain proapoptotic protein Bax of the Bcl-2 family is a central regulator for controlling the release of apoptogenic factors from mitochondria. Recent evidence suggests that the Bax-associating protein MOAP-1 may act as an effector for promoting Bax function in mitochondria. Here, we report that MOAP-1 protein is rapidly up-regulated by multiple apoptotic stimuli in mammalian cells. MOAP-1 is a short-lived protein (t(1/2) approximately 25 min) that is constitutively degraded by the ubiquitin-proteasome system. Induction of MOAP-1 by apoptotic stimuli ensues through inhibition of its polyubiquitination process. Elevation of MOAP-1 levels sensitizes cells to apoptotic stimuli and promotes recombinant Bax-mediated cytochrome c release from isolated mitochondria. Mitochondria depleted of short-lived proteins by cycloheximide (CHX) become resistant to Bax-mediated cytochrome c release. Remarkably, incubation of these mitochondria with in vitro-translated MOAP-1 effectively restores the cytochrome c releasing effect of recombinant Bax. We propose that apoptotic stimuli can facilitate the proapoptotic function of Bax in mitochondria through stabilization of MOAP-1. | lld:pubmed |
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| pubmed-article:17535899 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17535899 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17535899 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17535899 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17535899 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17535899 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17535899 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17535899 | pubmed:author | pubmed-author:SukumaranSuni... | lld:pubmed |
| pubmed-article:17535899 | pubmed:author | pubmed-author:YuVictor CVC | lld:pubmed |
| pubmed-article:17535899 | pubmed:author | pubmed-author:FuNai YangNY | lld:pubmed |
| pubmed-article:17535899 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17535899 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:17535899 | pubmed:volume | 104 | lld:pubmed |
| pubmed-article:17535899 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17535899 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17535899 | pubmed:pagination | 10051-6 | lld:pubmed |
| pubmed-article:17535899 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:17535899 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17535899 | pubmed:articleTitle | Inhibition of ubiquitin-mediated degradation of MOAP-1 by apoptotic stimuli promotes Bax function in mitochondria. | lld:pubmed |
| pubmed-article:17535899 | pubmed:affiliation | Institute of Molecular and Cell Biology, 61 Biopolis Drive (Proteos), Singapore 138673. | lld:pubmed |
| pubmed-article:17535899 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17535899 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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