Abstract |
The Fanconi anemia (FA) pathway, of which the FANCD2 protein is a key component, plays crucial roles in the maintenance of hematopoietic stem cells and suppression of carcinogenesis. However, the function of FANCD2 remains unclear. Here, we report that FANCD2 is a novel and specific substrate of caspase 3. Cleavage of FANCD2 by caspase 3 did not require either the FA core complex or mono-ubiquitylation of FANCD2, and was stimulated by p53. In addition, we identified the cleavage sites and generated cell lines that stably express a caspase-resistant FANCD2 mutant. Our data suggest that FANCD2 is regulated by caspase-mediated degradation during apoptosis induced by DNA damage.
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Authors | Wataru Sakai, Kaoru Sugasawa |
Journal | FEBS letters
(FEBS Lett)
Vol. 588
Issue 20
Pg. 3778-85
(Oct 16 2014)
ISSN: 1873-3468 [Electronic] England |
PMID | 25176410
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2014 The Authors. Published by Elsevier B.V. All rights reserved. |
Chemical References |
- BRCA2 Protein
- BRCA2 protein, human
- Tumor Suppressor Protein p53
- Caspase 3
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Topics |
- Apoptosis
- BRCA2 Protein
(genetics, metabolism)
- Caspase 3
(metabolism)
- DNA Damage
- HCT116 Cells
- HeLa Cells
- Humans
- Tumor Suppressor Protein p53
(metabolism)
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