Working together and apart: The twisted relationship of the Mre11 complex and Chk2 in apoptosis and tumor suppression Journal Article
| Authors: | Stracker, T. H.; Petrini, J. H. J. |
| Article Title: | Working together and apart: The twisted relationship of the Mre11 complex and Chk2 in apoptosis and tumor suppression |
| Abstract: | Central to the DNA damage response (DDR) is the highly conserved Mre11 complex consisting of Mre11, Rad50 and Nbs1. The Mre11 complex acts as a sensor of DNA double-strand breaks (DSBs) and regulates the signal transduction cascades that are triggered following damage detection.1 Rare human genetic instability syndromes such as Ataxia-telangiectasia (A-T) and Nijmegen Breakage Syndrome (NBS) have underscored the importance of the DSB response in the suppression of tumorigenesis, as well as other severe pathologies affecting the development of both the immune system and the central nervous system. Using murine models of the human diseases, we have investigated the role of the Mre11 complex, and other modulators of the DSB response, in tumor suppression. 2,3 We found that the checkpoint kinase Chk2 is crucial for the suppression of a diverse array of tumor types in Mre11 complex mutants and uncovered multiple roles for the Mre11 complex in apoptotic signaling in parallel to Chk2.4,5 ©2008 Landes Bioscience. |
| Keywords: | unclassified drug; dna-binding proteins; review; nonhuman; neoplasms; animals; cell cycle proteins; mice; dna damage; mre11; nbs1; rad50; apoptosis; models, biological; protein interaction; protein p53; cancer inhibition; b cell lymphoma; t cell lymphoma; protein-serine-threonine kinases; tumor suppressor proteins; murinae; atm protein; dna breaks, double-stranded; tumor suppressor protein p53; nijmegen breakage syndrome; double stranded dna break; checkpoint kinase 2; brca1; ataxia telangiectasia; chk2; deoxyribonucleoprotein; protien mre11 |
| Journal Title: | Cell Cycle |
| Volume: | 7 |
| Issue: | 23 |
| ISSN: | 1538-4101 |
| Publisher: | Taylor & Francis Inc. |
| Date Published: | 2008-12-01 |
| Start Page: | 3618 |
| End Page: | 3621 |
| Language: | English |
| PUBMED: | 19029802 |
| PROVIDER: | scopus |
| PMCID: | PMC2994099 |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 4" - "Export Date: 17 November 2011" - "Source: Scopus" |
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