DC Field | Value | Language |
---|---|---|
dc.contributor.author | Won, J | ko |
dc.contributor.author | Kim, DY | ko |
dc.contributor.author | La, M | ko |
dc.contributor.author | Kim, D | ko |
dc.contributor.author | Meadows, GG | ko |
dc.contributor.author | Joe, Cheol O | ko |
dc.date.accessioned | 2013-03-04T15:52:57Z | - |
dc.date.available | 2013-03-04T15:52:57Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-05 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, no.21, pp.19347 - 19351 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/83136 | - |
dc.description.abstract | The 14-3-3epsilon protein was identified as one of the caspase-3 substrates by the modified yeast two-hybrid system. The cellular 14-3-3epsilon protein was also cleaved in response to the treatment of apoptosis inducers in cultured mammalian cells. Asp(238) of the 14-3-3epsilon protein was determined as the site of cleavage by caspase-3. The affinity of the cleaved 14-3-3 mutant protein (D238) to Bad, a death-promoting Bcl-2 family protein, was lower than that of wild type or the uncleavable mutant 14-3-3epsilon protein (D238A). However, Bad associated with the cellular Bcl-x(L) more effectively in human 293T cells coexpressing Bad with the truncated form of the 14-3-3epsilon protein ( D238) than in control cells co-expressing Bad with wild type or the uncleavable mutant 14-3-3epsilon protein ( D238A). The present study suggests that the cleavage of 14-3-3 protein during apoptosis promotes cell death by releasing the associated Bad from the 14-3-3 protein and facilitates Bad translocation to the mitochondria and its interaction with Bcl-x(L). | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | PROMOTES CELL-SURVIVAL | - |
dc.subject | CYTOCHROME-C | - |
dc.subject | SIGNALING PROTEINS | - |
dc.subject | MITOCHONDRIA | - |
dc.subject | KINASE | - |
dc.subject | DEATH | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | BINDING | - |
dc.subject | RELEASE | - |
dc.subject | COMPLEXES | - |
dc.title | Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis | - |
dc.type | Article | - |
dc.identifier.wosid | 000182932200082 | - |
dc.identifier.scopusid | 2-s2.0-0038482014 | - |
dc.type.rims | ART | - |
dc.citation.volume | 278 | - |
dc.citation.issue | 21 | - |
dc.citation.beginningpage | 19347 | - |
dc.citation.endingpage | 19351 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.contributor.localauthor | Joe, Cheol O | - |
dc.contributor.nonIdAuthor | Won, J | - |
dc.contributor.nonIdAuthor | Kim, DY | - |
dc.contributor.nonIdAuthor | La, M | - |
dc.contributor.nonIdAuthor | Kim, D | - |
dc.contributor.nonIdAuthor | Meadows, GG | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | PROMOTES CELL-SURVIVAL | - |
dc.subject.keywordPlus | CYTOCHROME-C | - |
dc.subject.keywordPlus | SIGNALING PROTEINS | - |
dc.subject.keywordPlus | MITOCHONDRIA | - |
dc.subject.keywordPlus | KINASE | - |
dc.subject.keywordPlus | DEATH | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | RELEASE | - |
dc.subject.keywordPlus | COMPLEXES | - |
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