|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
13
|
|
pubmed:dateCreated |
2007-7-9
|
|
pubmed:abstractText |
The signaling of DNA damage and replication stress involves a multitude of proteins, including the kinases ataxia-telangiectasia mutated (ATM) and ATM and Rad3-related (ATR), and proteins with BRCA1 COOH-terminal (BRCT) domains. The BRCT domain-containing proteins facilitate the phosphorylation of ATM/ATR substrates and can be coimmunoprecipitated with ATM or ATR. However, their mode of interaction with the ATM/ATR kinases remains elusive. Here, we show that breast-ovarian cancer susceptibility 1 (BRCA1) interacts directly with ATR-interacting protein (ATRIP), an obligate partner of ATR. The interaction involves the BRCT domains of BRCA1 and Ser(239) of ATRIP, a residue that is phosphorylated in both irradiated and nonirradiated cells. Consistent with a role of BRCA1 in ATR signaling, substitution of Ser(239) of ATRIP with Ala leads to a G(2)-M checkpoint defect. We propose that a direct physical interaction between BRCA1 and ATRIP is required for the checkpoint function of ATR.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ATRIP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/BRCA1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/BRCA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/three prime repair exonuclease 1
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0008-5472
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
67
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
6100-5
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:17616665-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17616665-Amino Acid Sequence,
pubmed-meshheading:17616665-BRCA1 Protein,
pubmed-meshheading:17616665-Breast Neoplasms,
pubmed-meshheading:17616665-Cell Cycle Proteins,
pubmed-meshheading:17616665-DNA Damage,
pubmed-meshheading:17616665-DNA-Binding Proteins,
pubmed-meshheading:17616665-Exodeoxyribonucleases,
pubmed-meshheading:17616665-Female,
pubmed-meshheading:17616665-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:17616665-Genetic Predisposition to Disease,
pubmed-meshheading:17616665-Humans,
pubmed-meshheading:17616665-Molecular Sequence Data,
pubmed-meshheading:17616665-Ovarian Neoplasms,
pubmed-meshheading:17616665-Phosphoproteins,
pubmed-meshheading:17616665-Phosphorylation,
pubmed-meshheading:17616665-Protein-Serine-Threonine Kinases,
pubmed-meshheading:17616665-Sequence Homology, Amino Acid,
pubmed-meshheading:17616665-Serine
|
|
pubmed:year |
2007
|
|
pubmed:articleTitle |
Phosphorylation of ATR-interacting protein on Ser239 mediates an interaction with breast-ovarian cancer susceptibility 1 and checkpoint function.
|
|
pubmed:affiliation |
Wistar Institute, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
