Rif1 Prevents Resection of DNA Breaks and Promotes Immunoglobulin Class Switching
Copyright policy )Rif1 Prevents Resection of DNA Breaks and Promotes Immunoglobulin Class Switching
Fixing Broken DNA Some physiological processes, such as immunoglobulin class switching and telomere attrition, result in double-stranded DNA breaks. The DNA damage repair protein, 53BP1, prevents nucleolytic processing of these breaks, but the proteins it partners with to do this are unknown (see the Perspective by Lukas and Luka s ). Di Virgilio et al. (p. 711 , published online 10 January), using mass spectroscopy–based methods, and Zimmermann et al. (p. 700 , published online 10 January), using a telomere-based assay, identify Rif1 as a 53BP1 phosphorylation- and DNA damage–dependent interaction partner. Mice with a B cell–specific deletion in Rif1 showed impaired immunoglobulin class switching. Rif1-deficient cells exhibited extensive 5′-3′ resection at DNA ends, with enhanced genetic instability. Thus, Rif1 partners with 53BP1 to promote the proper repair of double-stranded DNA breaks.
- National Institutes of Health United States
- UNIVERSIDADE DE SAO PAULO Brazil
- National Institute of Arthritis and Musculoskeletal and Skin Diseases United States
- National Institute of Health Pakistan
- Universidade de São Paulo Brazil
G2 Phase, B-Lymphocytes, DNA Repair, Chromosomal Proteins, Non-Histone, Tumor Suppressor Proteins, Telomere-Binding Proteins, G1 Phase, Cell Cycle Proteins, Ataxia Telangiectasia Mutated Proteins, DNA, Protein Serine-Threonine Kinases, Immunoglobulin Class Switching, Genomic Instability, S Phase, DNA-Binding Proteins, Mice, Animals, DNA Breaks, Double-Stranded, Phosphorylation, Cells, Cultured
G2 Phase, B-Lymphocytes, DNA Repair, Chromosomal Proteins, Non-Histone, Tumor Suppressor Proteins, Telomere-Binding Proteins, G1 Phase, Cell Cycle Proteins, Ataxia Telangiectasia Mutated Proteins, DNA, Protein Serine-Threonine Kinases, Immunoglobulin Class Switching, Genomic Instability, S Phase, DNA-Binding Proteins, Mice, Animals, DNA Breaks, Double-Stranded, Phosphorylation, Cells, Cultured
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