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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-2-17
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pubmed:abstractText |
c-Abl protein tyrosine kinase plays an important role in cell cycle control and apoptosis. Furthermore, induction of apoptosis correlates with the activation of c-Abl. Here, we demonstrate the cleavage of c-Abl by caspases during apoptosis. Caspases separate c-Abl into functional domains including a Src-kinase, a fragment containing nuclear import sequences, a fragment with an actin-binding domain and nuclear export sequence. Caspase cleavage increases the kinase activity of c-Abl as demonstrated by in vitro kinase assays as well as by auto- and substrate phosphorylation. Cells in which c-Abl expression was knocked down by RNA interference resisted cisplatin- but not TNFalpha-induced apoptosis. A similar selective resistance against cisplatin-induced apoptosis was observed when cleavage resistant c-Abl was overexpressed in treated cells. Our data suggest the selective requirement of c-Abl cleavage by caspases for stress-induced, but not for TNFalpha-induced apoptosis.
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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 |
Mar
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pubmed:issn |
1350-9047
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
290-300
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14657961-Amino Acid Motifs,
pubmed-meshheading:14657961-Amino Acid Sequence,
pubmed-meshheading:14657961-Animals,
pubmed-meshheading:14657961-Antibodies, Monoclonal,
pubmed-meshheading:14657961-Apoptosis,
pubmed-meshheading:14657961-Blotting, Western,
pubmed-meshheading:14657961-Caspases,
pubmed-meshheading:14657961-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:14657961-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:14657961-Enzyme Activation,
pubmed-meshheading:14657961-Fluorescent Antibody Technique, Direct,
pubmed-meshheading:14657961-HeLa Cells,
pubmed-meshheading:14657961-Humans,
pubmed-meshheading:14657961-Jurkat Cells,
pubmed-meshheading:14657961-Mice,
pubmed-meshheading:14657961-Microscopy, Confocal,
pubmed-meshheading:14657961-Molecular Sequence Data,
pubmed-meshheading:14657961-NIH 3T3 Cells,
pubmed-meshheading:14657961-Polymerase Chain Reaction,
pubmed-meshheading:14657961-Precipitin Tests,
pubmed-meshheading:14657961-Protein Kinases,
pubmed-meshheading:14657961-Protein Structure, Tertiary,
pubmed-meshheading:14657961-Proto-Oncogene Proteins c-abl,
pubmed-meshheading:14657961-RNA Interference,
pubmed-meshheading:14657961-Sequence Homology, Amino Acid,
pubmed-meshheading:14657961-Stress, Physiological,
pubmed-meshheading:14657961-U937 Cells
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pubmed:year |
2004
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pubmed:articleTitle |
Requirement of caspase-mediated cleavage of c-Abl during stress-induced apoptosis.
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pubmed:affiliation |
Department of Molecular Biology, Max Planck Institute for Infection Biology, Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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