CtIP: A DNA damage response protein at the intersection of DNA metabolism

Nodar Makharashvili; Tanya T Paull

doi:10.1016/j.dnarep.2015.04.016

CtIP: A DNA damage response protein at the intersection of DNA metabolism

DNA Repair (Amst). 2015 Aug:32:75-81. doi: 10.1016/j.dnarep.2015.04.016. Epub 2015 May 2.

Authors

Nodar Makharashvili¹, Tanya T Paull²

Affiliations

¹ The Howard Hughes Medical Institute, The Department of Molecular Genetics and Microbiology, The Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA.
² The Howard Hughes Medical Institute, The Department of Molecular Genetics and Microbiology, The Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: tpaull@utexas.edu.

PMID: 25957490
DOI: 10.1016/j.dnarep.2015.04.016

Abstract

The mammalian CtIP protein and its orthologs in other eukaryotes promote the resection of DNA double-strand breaks and are essential for meiotic recombination. Here we review the current literature supporting the role of CtIP in DNA end processing and the importance of CtIP endonuclease activity in DNA repair. We also examine the regulation of CtIP function by post-translational modifications, and its involvement in transcription- and replication-dependent functions through association with other protein complexes. The tumor suppressor function of CtIP likely is dependent on a combination of these roles in many aspects of DNA metabolism.

Keywords: CtIP; DNA damage response; Double-strand break; Mre11/Rad50/Nbs1; Resection.

Publication types

Review

MeSH terms

Animals
Carrier Proteins / chemistry*
Carrier Proteins / genetics
Carrier Proteins / metabolism
DNA / chemistry
DNA / metabolism*
DNA Breaks, Double-Stranded*
DNA Breaks, Single-Stranded
DNA End-Joining Repair*
DNA, Single-Stranded / chemistry
DNA, Single-Stranded / metabolism
Endodeoxyribonucleases
Endonucleases / chemistry
Endonucleases / genetics
Endonucleases / metabolism
Homologous Recombination*
Humans
Nuclear Proteins / chemistry*
Nuclear Proteins / genetics
Nuclear Proteins / metabolism
Protein Processing, Post-Translational*
Protein Structure, Tertiary
Saccharomyces cerevisiae / genetics
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / chemistry
Saccharomyces cerevisiae Proteins / genetics
Saccharomyces cerevisiae Proteins / metabolism
Signal Transduction
Tumor Suppressor Proteins / chemistry
Tumor Suppressor Proteins / genetics
Tumor Suppressor Proteins / metabolism

Substances

Carrier Proteins
DNA, Single-Stranded
Nuclear Proteins
SAE2 protein, S cerevisiae
Saccharomyces cerevisiae Proteins
Tumor Suppressor Proteins
DNA
Endodeoxyribonucleases
Endonucleases
RBBP8 protein, human