rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
2001-6-25
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pubmed:abstractText |
Eukaryotic initiation factor (eIF) 4B interacts with several components of the initiation pathway and is targeted for cleavage during apoptosis. In a cell-free system, cleavage of eIF4B by caspase-3 coincides with a general inhibition of protein synthetic activity. Affinity chromatography demonstrates that mammalian eIF4B interacts with the poly(A)-binding protein and that a region consisting of the N-terminal 80 amino acids of eIF4B is both necessary and sufficient for such binding. This interaction is lost when eIF4B is cleaved by caspase-3, which removes the N-terminal 45 amino acids. Similarly, the association of eIF4B with the poly(A)-binding protein in vivo is reduced when cells are induced to undergo apoptosis. Cleavage of the poly(A)-binding protein itself, using human rhinovirus 3C protease, also eliminates the interaction with eIF4B. Thus, disruption of the association between mammalian eIF4B and the poly(A)-binding protein can occur during both apoptosis and picornaviral infection and is likely to contribute to the inhibition of translation observed under these conditions.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/3C proteases,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(A)-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-4B
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23922-8
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pubmed:dateRevised |
2007-10-11
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pubmed:meshHeading |
pubmed-meshheading:11274152-Amino Acid Sequence,
pubmed-meshheading:11274152-Apoptosis,
pubmed-meshheading:11274152-Caspase 3,
pubmed-meshheading:11274152-Caspases,
pubmed-meshheading:11274152-Cysteine Endopeptidases,
pubmed-meshheading:11274152-Eukaryotic Initiation Factors,
pubmed-meshheading:11274152-Humans,
pubmed-meshheading:11274152-Jurkat Cells,
pubmed-meshheading:11274152-Models, Biological,
pubmed-meshheading:11274152-Peptide Initiation Factors,
pubmed-meshheading:11274152-Picornaviridae Infections,
pubmed-meshheading:11274152-Poly(A)-Binding Proteins,
pubmed-meshheading:11274152-Protein Biosynthesis,
pubmed-meshheading:11274152-RNA-Binding Proteins,
pubmed-meshheading:11274152-Viral Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages.
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pubmed:affiliation |
Department of Biochemistry and Immunology, Cellular and Molecular Sciences Group, St. George's Hospital Medical School, Cranmer Terrace, London SW17 0RE, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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