| pubmed-article:17470634 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C1414119 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C1421412 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C1157990 | lld:lifeskim |
| pubmed-article:17470634 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:17470634 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17470634 | pubmed:dateCreated | 2007-5-8 | lld:pubmed |
| pubmed-article:17470634 | pubmed:abstractText | Dynamin-related protein 1 (DRP1) plays an important role in mitochondrial fission at steady state and during apoptosis. Using fluorescence recovery after photobleaching, we demonstrate that in healthy cells, yellow fluorescent protein (YFP)-DRP1 recycles between the cytoplasm and mitochondria with a half-time of 50 s. Strikingly, during apoptotic cell death, YFP-DRP1 undergoes a transition from rapid recycling to stable membrane association. The rapid cycling phase that characterizes the early stages of apoptosis is independent of Bax/Bak. However, after Bax recruitment to the mitochondrial membranes but before the loss of mitochondrial membrane potential, YFP-DRP1 becomes locked on the membrane, resulting in undetectable fluorescence recovery. This second phase in DRP1 cycling is dependent on the presence of Bax/Bak but independent of hFis1 and mitochondrial fragmentation. Coincident with Bax activation, we detect a Bax/Bak-dependent stimulation of small ubiquitin-like modifier-1 conjugation to DRP1, a modification that correlates with the stable association of DRP1 with mitochondrial membranes. Altogether, these data demonstrate that the apoptotic machinery regulates the biochemical properties of DRP1 during cell death. | lld:pubmed |
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| pubmed-article:17470634 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17470634 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17470634 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17470634 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17470634 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17470634 | pubmed:month | May | lld:pubmed |
| pubmed-article:17470634 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:17470634 | pubmed:author | pubmed-author:WasiakSylwiaS | lld:pubmed |
