pubmed-article:12813029 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C0090388 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C0086168 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1421563 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1417014 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1418407 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1424881 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1825938 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:12813029 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:12813029 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:12813029 | pubmed:dateCreated | 2003-6-18 | lld:pubmed |
pubmed-article:12813029 | pubmed:abstractText | TNF-alpha activates ASK1 in part by dissociating 14-3-3 from apoptosis signal-regulating kinase 1 (ASK1). In the present study, we identified a novel Ras GTPase-activating protein (Ras-GAP) as an ASK1-interacting protein (AIP1). AIP1 binds to the C-terminal domain of ASK1 via a lysine-rich cluster within the N-terminal C2 domain. AIP1 exists in a closed form through an intramolecular interaction between the N-terminus and the C-terminus, and TNF-alpha induces unfolding of AIP1 leading to association of AIP1 with ASK1. Thus, the N-terminus of AIP1 containing the C2 and GAP domains constitutively binds to ASK1 and facilitates the release of 14-3-3 from ASK1. In contrast to 14-3-3, AIP1 binds preferentially to dephosphorylated ASK1. Recruited AIP1 enhances ASK1-induced JNK activation, and the ASK1 binding and the GAP activity of AIP1 are critical for AIP1-enhanced ASK1 activation. Furthermore, TNF-induced ASK1/JNK activation is significantly blunted in cells where AIP1 is knocked down by RNA interference. These data suggest that AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of inhibitor 14-3-3 from ASK1, a novel mechanism by which TNF-alpha activates ASK1. | lld:pubmed |
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pubmed-article:12813029 | pubmed:language | eng | lld:pubmed |
pubmed-article:12813029 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12813029 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:12813029 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12813029 | pubmed:month | Jun | lld:pubmed |
pubmed-article:12813029 | pubmed:issn | 0021-9738 | lld:pubmed |
pubmed-article:12813029 | pubmed:author | pubmed-author:WebbS LSL | lld:pubmed |
pubmed-article:12813029 | pubmed:author | pubmed-author:ZhangRongR | lld:pubmed |
pubmed-article:12813029 | pubmed:author | pubmed-author:HsiehJer-Tson... | lld:pubmed |
pubmed-article:12813029 | pubmed:author | pubmed-author:LiuWeiminW | lld:pubmed |
pubmed-article:12813029 | pubmed:author | pubmed-author:MengLuL | lld:pubmed |
pubmed-article:12813029 | pubmed:author | pubmed-author:HeXiangrongX | lld:pubmed |
pubmed-article:12813029 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12813029 | pubmed:volume | 111 | lld:pubmed |
pubmed-article:12813029 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12813029 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12813029 | pubmed:pagination | 1933-43 | lld:pubmed |
pubmed-article:12813029 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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pubmed-article:12813029 | pubmed:meshHeading | pubmed-meshheading:12813029... | lld:pubmed |
pubmed-article:12813029 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12813029 | pubmed:articleTitle | AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3. | lld:pubmed |
pubmed-article:12813029 | pubmed:affiliation | Center for Cardiovascular Research, University of Rochester Medical Center, Rochester, New York 14642, USA. | lld:pubmed |
pubmed-article:12813029 | pubmed:publicationType | Journal Article | lld:pubmed |