| pubmed-article:18180367 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C0010834 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C1414371 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C0527839 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C1421894 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C1326203 | lld:lifeskim |
| pubmed-article:18180367 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:18180367 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18180367 | pubmed:dateCreated | 2008-1-15 | lld:pubmed |
| pubmed-article:18180367 | pubmed:abstractText | The RNA-binding protein HuR affects cell fate by regulating the stability and/or the translation of messenger RNAs that encode cell stress response proteins. In this study, we delineate a novel regulatory mechanism by which HuR contributes to stress-induced cell death. Upon lethal stress, HuR translocates into the cytoplasm by a mechanism involving its association with the apoptosome activator pp32/PHAP-I. Depleting the expression of pp32/PHAP-I by RNA interference reduces both HuR cytoplasmic accumulation and the efficiency of caspase activation. In the cytoplasm, HuR undergoes caspase-mediated cleavage at aspartate 226. This cleavage activity is significantly reduced in the absence of pp32/PHAP-I. Substituting aspartate 226 with an alanine creates a noncleavable isoform of HuR that, when overexpressed, maintains its association with pp32/PHAP-I and delays the apoptotic response. Thus, we propose a model in which HuR association with pp32/PHAP-I and its caspase-mediated cleavage constitutes a regulatory step that contributes to an amplified apoptotic response. | lld:pubmed |
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| pubmed-article:18180367 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18180367 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18180367 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18180367 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18180367 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18180367 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18180367 | pubmed:issn | 1540-8140 | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:TenenbaumScot... | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:KeeneJack DJD | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:MazrouiRachid... | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:Di... | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:ClairEvelineE | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:SalehMayaM | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:GallouziImed-... | lld:pubmed |
| pubmed-article:18180367 | pubmed:author | pubmed-author:von... | lld:pubmed |
| pubmed-article:18180367 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18180367 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:18180367 | pubmed:volume | 180 | lld:pubmed |
| pubmed-article:18180367 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18180367 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18180367 | pubmed:pagination | 113-27 | lld:pubmed |
| pubmed-article:18180367 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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