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...

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Main Authors: Calonge Teresa M, Tapia-Alveal Claudia, O'Connell Matthew J
Format: Article
Language:English
Published: BMC 2009-04-01
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>
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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