BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting

Science

Volumn 302, Issue 5645, 2003, Pages 636-639

  Manke, Isaac A ^a   Lowery, Drew M ^a   Nguyen, Anhco ^a   Yaffe, Michael B ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; IRRADIATION; MUTAGENESIS; TUMORS;

SIGNAL TRANSDUCTION;

PROTEINS;

53BP1 PROTEIN; ATM PROTEIN; ATR PROTEIN; BRCA1 PROTEIN; BRCT PROTEIN; PAX TRANSACTIVATION DOMAIN INTERACTING PROTEIN; PEPTIDE LIBRARY; PHOSPHOH2AX PROTEIN; PHOSPHOPEPTIDE; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTRANSFERASE; PROTEIN; UNCLASSIFIED DRUG;

BIOLOGY; CANCER; DNA; PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BREAST CANCER; CARBOXY TERMINAL SEQUENCE; DNA DAMAGE; DNA LIBRARY; FEMALE; GAMMA IRRADIATION; GENETIC PREDISPOSITION; HUMAN; OVARY CANCER; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; PROTEOMICS; SIGNAL TRANSDUCTION;

AMINO ACID MOTIFS; BRCA1 PROTEIN; CAFFEINE; CALORIMETRY; CARRIER PROTEINS; CELL CYCLE PROTEINS; CELL NUCLEUS; CYTOSOL; DNA DAMAGE; DNA-BINDING PROTEINS; GAMMA RAYS; HUMANS; NUCLEAR PROTEINS; PEPTIDE LIBRARY; PHOSPHOPEPTIDES; PHOSPHORYLATION; PHOSPHOSERINE; PHOSPHOTHREONINE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; PROTEOMICS; SIGNAL TRANSDUCTION; TUMOR CELLS, CULTURED; TUMOR SUPPRESSOR PROTEINS;

ATAXIA; ATAXIA TELANGIECTASIA;

EID: 0142240342     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1088877     Document Type: Article

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25. We thank K. Hoepker and A. Elia for participation at early stages in this work, T. Ho and S. Bissonnette for figure construction, D. Rubinson and J. Loureiro for assistance with microscopy, R. Grant for assistance with protein purification, J. Robbins for critical reading of the manuscript, R. T. Abraham for discussions, and J. Chen for sharing unpublished data. The MDC1, 53BP1, and Brca1 plasmids were gifts from S. J. Elledge, K. Iwabuchi, and D. Livingston, respectively. D.M.L is a Howard Hughes Medical Institute predoctoral fellow. Supported by NIH grant GM60594 and a Burroughs-Wellcome Career Development Award (M.B.Y.).