Open Access

Nature Communications, volume 7, issue 1, publication number 10881

TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions

Rai Rekha ¹

Chen Yong ²

Lei Ming ²

Chang Sandy ^{1, 3, 4}

Hide authors affiliations Show authors affiliations: 4 affiliations

Department of Laboratory Medicine, Yale University School of Medicine, New Haven, USA |

National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China |

Department of Pathology, Yale University School of Medicine, New Haven, USA |

⁴

Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, USA |

Publication type: Journal Article

Publication date: 2016-03-04

Springer Nature

Journal: Nature Communications

Quartile SCImago

Quartile WOS

Impact factor: 16.6

ISSN: 20411723

DOI: 10.1038/ncomms10881

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PubMed ID: 26941064

General Chemistry

General Biochemistry, Genetics and Molecular Biology

General Physics and Astronomy

Abstract

Repressor/activator protein 1 (RAP1) is a highly conserved telomere-interacting protein. Yeast Rap1 protects telomeres from non-homologous end joining (NHEJ), plays important roles in telomere length control and is involved in transcriptional gene regulation. However, a role for mammalian RAP1 in telomere end protection remains controversial. Here we present evidence that mammalian RAP1 is essential to protect telomere from homology directed repair (HDR) of telomeres. RAP1 cooperates with the basic domain of TRF2 (TRF2B) to repress PARP1 and SLX4 localization to telomeres. Without RAP1 and TRF2B, PARP1 and SLX4 HR factors promote rapid telomere resection, resulting in catastrophic telomere loss and the generation of telomere-free chromosome fusions in both mouse and human cells. The RAP1 Myb domain is required to repress both telomere loss and formation of telomere-free fusions. Our results highlight the importance of the RAP1-TRF2 heterodimer in protecting telomeres from inappropriate processing by the HDR pathway.

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American Association for the Advancement of Science (AAAS)	American Association for the Advancement of Science (AAAS), 1, 1.02% American Association for the Advancement of Science (AAAS) 1 publication, 1.02%
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	2 4 6 8 10 12 14 16 18

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Rai R. et al. TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions // Nature Communications. 2016. Vol. 7. No. 1. 10881

GOST all authors (up to 50) Copy

Rai R., Chen Y., Lei M., Chang S. TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions // Nature Communications. 2016. Vol. 7. No. 1. 10881

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RIS Copy

TY - JOUR

DO - 10.1038/ncomms10881

UR - https://doi.org/10.1038%2Fncomms10881

TI - TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions

T2 - Nature Communications

AU - Rai, Rekha

AU - Chen, Yong

AU - Lei, Ming

AU - Chang, Sandy

PY - 2016

DA - 2016/03/04 00:00:00

PB - Springer Nature

IS - 1

VL - 7

PMID - 26941064

SN - 2041-1723

ER -

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@article{2016_Rai,

author = {Rekha Rai and Yong Chen and Ming Lei and Sandy Chang},

title = {TRF2-RAP1 is required to protect telomeres from engaging in homologous recombination-mediated deletions and fusions},

journal = {Nature Communications},

year = {2016},

volume = {7},

publisher = {Springer Nature},

month = {mar},

url = {https://doi.org/10.1038%2Fncomms10881},

number = {1},

doi = {10.1038/ncomms10881}

}

Found error?

Publisher

Springer Nature

Journal

Nature Communications

Quartile SCImago

Quartile WOS

Impact factor

16.6

ISSN

20411723 (Print)