Document Detail


Complementary functions of ATM and H2AX in development and suppression of genomic instability.
MedLine Citation:
PMID:  18599436     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Upon DNA damage, histone H2AX is phosphorylated by ataxia-telangiectasia mutated (ATM) and other phosphoinositide 3-kinase-related protein kinases. To elucidate further the potential overlapping and unique functions of ATM and H2AX, we asked whether they have synergistic functions in the development and maintenance of genomic stability by inactivating both genes in mouse germ line. Combined ATM/H2AX deficiency caused embryonic lethality and dramatic cellular genomic instability. Mechanistically, severe genomic instability in the double-deficient cells is associated with a requirement for H2AX to repair oxidative DNA damage resulting from ATM deficiency. We discuss these findings in the context of synergies between ATM and other repair factors.
Authors:
Shan Zha; JoAnn Sekiguchi; James W Brush; Craig H Bassing; Frederick W Alt
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2008-07-01
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  105     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2008 Jul 
Date Detail:
Created Date:  2008-07-14     Completed Date:  2008-08-08     Revised Date:  2011-11-02    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  9302-6     Citation Subset:  IM    
Affiliation:
Howard Hughes Medical Institute, Children's Hospital, Immune Disease Institute, Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Cycle Proteins / metabolism*
Cell Proliferation
DNA Damage
DNA Repair
DNA-Binding Proteins / metabolism*
Embryo Loss / metabolism
Embryo, Mammalian / abnormalities,  metabolism
Embryonic Stem Cells / metabolism
Female
Fibroblasts / metabolism,  pathology
Genomic Instability*
Histones / metabolism*
Mice
Pregnancy
Protein-Serine-Threonine Kinases / metabolism*
Reactive Oxygen Species / metabolism
Tumor Suppressor Proteins / metabolism*
Grant Support
ID/Acronym/Agency:
5P01 CA109901-03/CA/NCI NIH HHS; 5P01 CA92625-06/CA/NCI NIH HHS; 5P01CA92625-06/CA/NCI NIH HHS; 5R01 CA125195-02/CA/NCI NIH HHS; R01 CA125195-02/CA/NCI NIH HHS; R01 CA125195-05/CA/NCI NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/DNA-Binding Proteins; 0/H2AX protein, mouse; 0/Histones; 0/Reactive Oxygen Species; 0/Tumor Suppressor Proteins; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/ataxia telangiectasia mutated protein
Comments/Corrections

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