| pubmed-article:17724464 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17724464 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:17724464 | lifeskim:mentions | umls-concept:C1366587 | lld:lifeskim |
| pubmed-article:17724464 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
| pubmed-article:17724464 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:17724464 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17724464 | pubmed:dateCreated | 2008-2-28 | lld:pubmed |
| pubmed-article:17724464 | pubmed:abstractText | The prosurvival Bcl-2-family member Bfl-1/A1 is a transcriptional target of nuclear factor-kappaB (NF-kappaB) that is overexpressed in many human tumors and is a means by which NF-kappaB inhibits apoptosis, but its mode of action is controversial. To better understand how Bfl-1 functions, we investigated its interaction with proapoptotic multidomain proteins Bax and Bak, and the BH3-only proteins Bid and tBid. We demonstrate that in living cells Bfl-1 selectively interacts with Bak and tBid, but not with Bax or Bid. Bfl-1/Bak interaction is functional as Bfl-1 suppressed staurosporine (STS)-induced apoptosis in wild-type and Bax-deficient cells, but not in Bak-/- cells. We also show that Bfl-1 blocks tumor necrosis factor-alpha (TNFalpha)-induced activation of Bax indirectly, via association with tBid. C-terminal deletion decreased Bfl-1's interaction with Bak and tBid and reduced its ability to suppress Bak- and tBid-mediated cell death. These data indicate that Bfl-1 utilizes different mechanisms to suppress apoptosis depending on the stimulus. Bfl-1 associates with tBid to prevent activation of proapoptotic Bax and Bak, and it also interacts directly with Bak to antagonize Bak-mediated cell death, similar to Mcl-1. Thus, part of the protective function of NF-kappaB is to induce Mcl-1-like activity by upregulating Bfl-1. | lld:pubmed |
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| pubmed-article:17724464 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17724464 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17724464 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17724464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17724464 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17724464 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17724464 | pubmed:issn | 1476-5594 | lld:pubmed |
| pubmed-article:17724464 | pubmed:author | pubmed-author:WhiteEE | lld:pubmed |
| pubmed-article:17724464 | pubmed:author | pubmed-author:GélinasCC | lld:pubmed |
| pubmed-article:17724464 | pubmed:author | pubmed-author:SimmonsM JMJ | lld:pubmed |
| pubmed-article:17724464 | pubmed:author | pubmed-author:FayJJ | lld:pubmed |
| pubmed-article:17724464 | pubmed:author | pubmed-author:DegenhardtKK | lld:pubmed |
| pubmed-article:17724464 | pubmed:author | pubmed-author:ZongW-XWX | lld:pubmed |
| pubmed-article:17724464 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17724464 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:17724464 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:17724464 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17724464 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17724464 | pubmed:pagination | 1421-8 | lld:pubmed |
| pubmed-article:17724464 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:17724464 | pubmed:meshHeading | pubmed-meshheading:17724464... | lld:pubmed |
| pubmed-article:17724464 | pubmed:meshHeading | pubmed-meshheading:17724464... | lld:pubmed |
| pubmed-article:17724464 | pubmed:meshHeading | pubmed-meshheading:17724464... | lld:pubmed |
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| pubmed-article:17724464 | pubmed:meshHeading | pubmed-meshheading:17724464... | lld:pubmed |
| pubmed-article:17724464 | pubmed:meshHeading | pubmed-meshheading:17724464... | lld:pubmed |
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| pubmed-article:17724464 | pubmed:meshHeading | pubmed-meshheading:17724464... | lld:pubmed |
| pubmed-article:17724464 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:17724464 | pubmed:articleTitle | Bfl-1/A1 functions, similar to Mcl-1, as a selective tBid and Bak antagonist. | lld:pubmed |
| pubmed-article:17724464 | pubmed:affiliation | Center for Advanced Biotechnology and Medicine, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854-5638, USA. | lld:pubmed |
| pubmed-article:17724464 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17724464 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:17724464 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17724464 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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