| pubmed-article:15366927 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C0558356 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C1418406 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C1418407 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C1424881 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C1825938 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C0752218 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:15366927 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:15366927 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:15366927 | pubmed:dateCreated | 2004-9-15 | lld:pubmed |
| pubmed-article:15366927 | pubmed:abstractText | Apoptosis-linked gene-2 (ALG-2) encodes a 22 kDa Ca(2+)-binding protein of the penta EF-hand family that is required for programmed cell death in response to various apoptotic agents. Here, we demonstrate that ALG-2 mRNA and protein are down-regulated in human uveal melanoma cells compared to their progenitor cells, normal melanocytes. The down regulation of ALG-2 may provide melanoma cells with a selective advantage. ALG-2 and its putative target molecule, Alix/AIP1, are localized primarily in the cytoplasm of melanocytes and melanoma cells independent of the intracellular Ca(2+) concentration or the activation of apoptosis. Cross-linking and analytical centrifugation studies support a single-species dimer conformation of ALG-2, also independent of Ca(2+) concentration. However, binding of Ca(2+) to both EF-1 and EF-3 is necessary for ALG-2 interaction with Alix/AIP1 as demonstrated using surface plasmon resonance spectroscopy. Mutations in EF-5 result in reduced target interaction without alteration in Ca(2+) affinity. The addition of N-terminal ALG-2 peptides, residues 1-22 or residues 7-17, does not alter the interaction of ALG-2 or an N-terminal deletion mutant of ALG-2 with Alix/AIP1, as might be expected from a model derived from the crystal structure of ALG-2. Fluorescence studies of ALG-2 demonstrate that an increase in surface hydrophobicity is primarily due to Ca(2+) binding to EF-3, while Ca(2+) binding to EF-1 has little effect on surface exposure of hydrophobic residues. Together, these data indicate that gross surface hydrophobicity changes are insufficient for target recognition. | lld:pubmed |
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| pubmed-article:15366927 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15366927 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15366927 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15366927 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15366927 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:PalczewskiKrz... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:CrabbJohn WJW | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:DurusselIsabe... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:WalkerTeresa... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:SubramanianLa... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:PolansArthur... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:BhattacharyaS... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:AghaAmarA | lld:pubmed |
| pubmed-article:15366927 | pubmed:author | pubmed-author:DellariaJulia... | lld:pubmed |
| pubmed-article:15366927 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15366927 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:15366927 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:15366927 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15366927 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15366927 | pubmed:pagination | 11175-86 | lld:pubmed |
| pubmed-article:15366927 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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