rdf:type |
|
lifeskim:mentions |
umls-concept:C0012860,
umls-concept:C0033681,
umls-concept:C0033684,
umls-concept:C0086418,
umls-concept:C0851285,
umls-concept:C0871261,
umls-concept:C1155874,
umls-concept:C1419245,
umls-concept:C1704632,
umls-concept:C1704928,
umls-concept:C1706817,
umls-concept:C2911692
|
pubmed:issue |
10
|
pubmed:dateCreated |
2002-4-24
|
pubmed:abstractText |
The ubiquitously expressed c-Abl tyrosine kinase is activated in the apoptotic response of cells to DNA damage. The mechanisms by which c-Abl signals the induction of apoptosis are not understood. Here we show that c-Abl binds constitutively to the mammalian homolog of the Schizosaccharomyces pombe Rad9 cell cycle checkpoint protein. The SH3 domain of c-Abl interacts directly with the C-terminal region of Rad9. c-Abl phosphorylates the Rad9 Bcl-2 homology 3 domain (Tyr-28) in vitro and in cells exposed to DNA-damaging agents. The results also demonstrate that c-Abl-mediated phosphorylation of Rad9 induces binding of Rad9 to the antiapototic Bcl-x(L) protein. The regulation of Rad9 by c-Abl in the DNA damage response is further supported by the demonstration that the interaction between c-Abl and Rad9 contributes to DNA damage-induced apoptosis. These findings indicate that Rad9 is regulated by a c-Abl-dependent mechanism in the apoptotic response to genotoxic stress.
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pubmed:grant |
|
pubmed:commentsCorrections |
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0270-7306
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
22
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|