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rdf:type |
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lifeskim:mentions |
umls-concept:C0011065,
umls-concept:C0031715,
umls-concept:C0036720,
umls-concept:C0090388,
umls-concept:C0205169,
umls-concept:C0219472,
umls-concept:C0243192,
umls-concept:C0288331,
umls-concept:C0871261,
umls-concept:C1167622,
umls-concept:C1274040,
umls-concept:C1332397,
umls-concept:C1366450,
umls-concept:C1421563,
umls-concept:C1565114,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
4
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pubmed:dateCreated |
1997-1-2
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pubmed:abstractText |
Extracellular survival factors alter a cell's susceptibility to apoptosis, often through posttranslational mechanisms. However, no consistent relationship has been established between such survival signals and the BCL-2 family, where the balance of death agonists versus antagonists determines susceptibility. One distant member, BAD, heterodimerizes with BCL-X(L) or BCL-2, neutralizing their protective effect and promoting cell death. In the presence of survival factor IL-3, cells phosphorylated BAD on two serine residues embedded in 14-3-3 consensus binding sites. Only the nonphosphorylated BAD heterodimerized with BCL-X(L) at membrane sites to promote cell death. Phosphorylated BAD was sequestered in the cytosol bound to 14-3-3. Substitution of serine phosphorylation sites further enhanced BAD's death-promoting activity. The rapid phosphorylation of BAD following IL-3 connects a proximal survival signal with the BCL-2 family, modulating this checkpoint for apoptosis.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
619-28
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8929531-14-3-3 Proteins,
pubmed-meshheading:8929531-Amino Acid Sequence,
pubmed-meshheading:8929531-Carrier Proteins,
pubmed-meshheading:8929531-Cell Death,
pubmed-meshheading:8929531-Cell Survival,
pubmed-meshheading:8929531-Cytosol,
pubmed-meshheading:8929531-Dimerization,
pubmed-meshheading:8929531-Interleukin-3,
pubmed-meshheading:8929531-Membranes,
pubmed-meshheading:8929531-Models, Biological,
pubmed-meshheading:8929531-Molecular Sequence Data,
pubmed-meshheading:8929531-Phosphorylation,
pubmed-meshheading:8929531-Protein Binding,
pubmed-meshheading:8929531-Proteins,
pubmed-meshheading:8929531-Proto-Oncogene Proteins,
pubmed-meshheading:8929531-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:8929531-Serine,
pubmed-meshheading:8929531-Signal Transduction,
pubmed-meshheading:8929531-Tyrosine 3-Monooxygenase,
pubmed-meshheading:8929531-bcl-Associated Death Protein,
pubmed-meshheading:8929531-bcl-X Protein
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pubmed:year |
1996
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pubmed:articleTitle |
Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
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pubmed:affiliation |
Department of Medicine, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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