Regulation of Chk1
<p>Abstract</p> <p>Chk1 is a serine/threonine protein kinase that is the effector of the G2 DNA damage checkpoint. Chk1 homologs have a highly conserved N-terminal kinase domain, and a less conserved C-terminal regulatory domain of ~200 residues. In response to a variety of genomic...
Main Authors: | , , |
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Format: | Article |
Language: | English |
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BMC
2009-04-01
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Series: | Cell Division |
Online Access: | http://www.celldiv.com/content/4/1/8 |
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author | Calonge Teresa M Tapia-Alveal Claudia O'Connell Matthew J |
author_facet | Calonge Teresa M Tapia-Alveal Claudia O'Connell Matthew J |
author_sort | Calonge Teresa M |
collection | DOAJ |
description | <p>Abstract</p> <p>Chk1 is a serine/threonine protein kinase that is the effector of the G2 DNA damage checkpoint. Chk1 homologs have a highly conserved N-terminal kinase domain, and a less conserved C-terminal regulatory domain of ~200 residues. In response to a variety of genomic lesions, a number of proteins collaborate to activate Chk1, which in turn ensures that the mitotic cyclin-dependent kinase Cdc2 remains in an inactive state until DNA repair is completed. Chk1 activation requires the phosphorylation of residues in the C-terminal domain, and this is catalyzed by the ATR protein kinase. How phosphorylation of the C-terminal regulatory domain activates the N-terminal kinase domain has not been elucidated, though some studies have suggested that this phosphorylation relieves an inhibitory intramolecular interaction between the N- and C-termini. However, recent studies in the fission yeast <it>Schizosaccharomyces pombe </it>have revealed that there is more to Chk1 regulation than this auto-inhibition model, and we review these findings and their implication to the biology of this genome integrity determinant.</p> |
first_indexed | 2024-04-12T16:35:57Z |
format | Article |
id | doaj.art-bb3807aecc104e7e990639dc7dbeca0e |
institution | Directory Open Access Journal |
issn | 1747-1028 |
language | English |
last_indexed | 2024-04-12T16:35:57Z |
publishDate | 2009-04-01 |
publisher | BMC |
record_format | Article |
series | Cell Division |
spelling | doaj.art-bb3807aecc104e7e990639dc7dbeca0e2022-12-22T03:25:00ZengBMCCell Division1747-10282009-04-0141810.1186/1747-1028-4-8Regulation of Chk1Calonge Teresa MTapia-Alveal ClaudiaO'Connell Matthew J<p>Abstract</p> <p>Chk1 is a serine/threonine protein kinase that is the effector of the G2 DNA damage checkpoint. Chk1 homologs have a highly conserved N-terminal kinase domain, and a less conserved C-terminal regulatory domain of ~200 residues. In response to a variety of genomic lesions, a number of proteins collaborate to activate Chk1, which in turn ensures that the mitotic cyclin-dependent kinase Cdc2 remains in an inactive state until DNA repair is completed. Chk1 activation requires the phosphorylation of residues in the C-terminal domain, and this is catalyzed by the ATR protein kinase. How phosphorylation of the C-terminal regulatory domain activates the N-terminal kinase domain has not been elucidated, though some studies have suggested that this phosphorylation relieves an inhibitory intramolecular interaction between the N- and C-termini. However, recent studies in the fission yeast <it>Schizosaccharomyces pombe </it>have revealed that there is more to Chk1 regulation than this auto-inhibition model, and we review these findings and their implication to the biology of this genome integrity determinant.</p>http://www.celldiv.com/content/4/1/8 |
spellingShingle | Calonge Teresa M Tapia-Alveal Claudia O'Connell Matthew J Regulation of Chk1 Cell Division |
title | Regulation of Chk1 |
title_full | Regulation of Chk1 |
title_fullStr | Regulation of Chk1 |
title_full_unstemmed | Regulation of Chk1 |
title_short | Regulation of Chk1 |
title_sort | regulation of chk1 |
url | http://www.celldiv.com/content/4/1/8 |
work_keys_str_mv | AT calongeteresam regulationofchk1 AT tapiaalvealclaudia regulationofchk1 AT oconnellmatthewj regulationofchk1 |