Home LiteratureArticle Details
PMID: 10766245 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway.

Nature ·Vol. 404 ·No. 6778 ·2000-04-06 ·Pages 613-7

Lim DS, Kim ST, Xu B, Maser RS, Lin J, Petrini JH, Kastan MB

Abstract

The rare diseases ataxia-telangiectasia (AT), caused by mutations in the ATM gene, and Nijmegen breakage syndrome (NBS), with mutations in the p95/nbs1 gene, share a variety of phenotypic abnormalities such as chromosomal instability, radiation sensitivity and defects in cell-cycle checkpoints in response to ionizing radiation. The ATM gene encodes a protein kinase that is activated by ionizing radiation or radiomimetic drugs, whereas p95/nbs1 is part of a protein complex that is involved in responses to DNA double-strand breaks. Here, because of the similarities between AT and NBS, we evaluated the functional interactions between ATM and p95/nbs1. Activation of the ATM kinase by ionizing radiation and induction of ATM-dependent responses in NBS cells indicated that p95/nbs1 may not be required for signalling to ATM after ionizing radiation. However, p95/nbs1 was phosphorylated on serine 343 in an ATM-dependent manner in vitro and in vivo after ionizing radiation. A p95/nbs1 construct mutated at the ATM phosphorylation site abrogated an S-phase checkpoint induced by ionizing radiation in normal cells and failed to compensate for this functional deficiency in NBS cells. These observations link ATM and p95/nbs1 in a common signalling pathway and provide an explanation for phenotypic similarities in these two diseases.

MeSH Terms
Ataxia Telangiectasia Ataxia Telangiectasia Mutated Proteins Cell Cycle Proteins/genetics,metabolism Cell Line DNA/biosynthesis,radiation effects DNA-Binding Proteins Enzyme Activation/radiation effects Humans Mutagenesis Nuclear Proteins Phosphatidylinositol 3-Kinases/genetics,metabolism,radiation effects Phosphorylation Protein Serine-Threonine Kinases/genetics,metabolism,radiation effects Recombinant Fusion Proteins/genetics,metabolism S Phase Serine/metabolism Signal Transduction Transfection Tumor Suppressor Protein p53/metabolism Tumor Suppressor Proteins
Chemicals
Cell Cycle Proteins DNA-Binding Proteins NBN protein, human Nuclear Proteins Recombinant Fusion Proteins Tumor Suppressor Protein p53 Tumor Suppressor Proteins Serine DNA ATM protein, human Ataxia Telangiectasia Mutated Proteins Protein Serine-Threonine Kinases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Lim D S
Department of Hematology-Oncology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Kim S T
Xu B
Maser R S
Lin J
Petrini J H
Kastan M B
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
2000-04-06
Pages
613-7
Language
English
Region
England
NLM ID
0410462
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com