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| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C0086282 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C0376515 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C1366587 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C1511012 | lld:lifeskim |
| pubmed-article:10837489 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:10837489 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:10837489 | pubmed:dateCreated | 2000-9-21 | lld:pubmed |
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| pubmed-article:10837489 | pubmed:abstractText | MCL-1 (myeloid cell leukemia-1) is an antiapoptotic BCL-2 family protein discovered as an early induction gene during myeloblastic leukemia cell differentiation. This survival protein has the BCL-2 homology (BH) domains 1, 2, and 3 and a C-terminal transmembrane region. We identified a short splicing variant of the MCL-1 mRNA in the human placenta encoding a protein, termed MCL-1 short (MCL-1S), with an altered C terminus as compared with the full-length MCL-1 long (MCL-1L), leading to the loss of BH1, BH2, and the transmembrane domains. Analysis of the human MCL-1 gene indicated that MCL-1S results from the splicing out of exon 2 during mRNA processing. MCL-1S, unlike MCL-1L, does not interact with diverse proapoptotic BCL-2-related proteins in the yeast two-hybrid system. In contrast, MCL-1S dimerizes with MCL-1L in the yeast assay and coprecipitates with MCL-1L in transfected mammalian cells. Overexpression of MCL-1S induces apoptosis in transfected Chinese hamster ovary cells, and the MCL-1S action was antagonized by the antiapoptotic MCL-1L. Thus, the naturally occurring MCL-1S variant represents a new proapoptotic BH3 domain-only protein capable of dimerizing with the antiapoptotic MCL-1L. The fate of MCL-1-expressing cells could be regulated through alternative splicing mechanisms and interactions of the resulting anti- and proapoptotic gene products. | lld:pubmed |
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| pubmed-article:10837489 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10837489 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10837489 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10837489 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10837489 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10837489 | pubmed:author | pubmed-author:BalAA | lld:pubmed |
| pubmed-article:10837489 | pubmed:author | pubmed-author:HsuehA JAJ | lld:pubmed |
| pubmed-article:10837489 | pubmed:author | pubmed-author:HsuS YSY | lld:pubmed |
| pubmed-article:10837489 | pubmed:author | pubmed-author:LeeC FCF | lld:pubmed |
| pubmed-article:10837489 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10837489 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:10837489 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10837489 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10837489 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10837489 | pubmed:pagination | 25255-61 | lld:pubmed |
| pubmed-article:10837489 | pubmed:dateRevised | 2008-7-9 | lld:pubmed |
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| pubmed-article:10837489 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10837489 | pubmed:articleTitle | MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. | lld:pubmed |
| pubmed-article:10837489 | pubmed:affiliation | Division of Reproductive Biology, Department of Gynecology and Obstetrics, Stanford University School of Medicine, CA 94305-5317, USA. | lld:pubmed |
| pubmed-article:10837489 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10837489 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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