USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP

C-terminal binding protein (CtBP) interacting protein (CtIP) is a fundamental factor for the initiation of DNA end resection to initiate DNA repair. Here the authors reveal mechanistic insights into the regulation of CtIP via the deubiquitinase USP52.

Bibliographic Details
Main Authors: Ming Gao, Guijie Guo, Jinzhou Huang, Jake A. Kloeber, Fei Zhao, Min Deng, Xinyi Tu, Wootae Kim, Qin Zhou, Chao Zhang, Ping Yin, Kuntian Luo, Zhenkun Lou
Format: Article
Language:English
Published: Nature Portfolio 2020-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-19202-0
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author Ming Gao
Guijie Guo
Jinzhou Huang
Jake A. Kloeber
Fei Zhao
Min Deng
Xinyi Tu
Wootae Kim
Qin Zhou
Chao Zhang
Ping Yin
Kuntian Luo
Zhenkun Lou
author_facet Ming Gao
Guijie Guo
Jinzhou Huang
Jake A. Kloeber
Fei Zhao
Min Deng
Xinyi Tu
Wootae Kim
Qin Zhou
Chao Zhang
Ping Yin
Kuntian Luo
Zhenkun Lou
author_sort Ming Gao
collection DOAJ
description C-terminal binding protein (CtBP) interacting protein (CtIP) is a fundamental factor for the initiation of DNA end resection to initiate DNA repair. Here the authors reveal mechanistic insights into the regulation of CtIP via the deubiquitinase USP52.
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spelling doaj.art-0cbdcde06d9e49459d90c92d2584a8612022-12-21T19:07:36ZengNature PortfolioNature Communications2041-17232020-10-0111111310.1038/s41467-020-19202-0USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIPMing Gao0Guijie Guo1Jinzhou Huang2Jake A. Kloeber3Fei Zhao4Min Deng5Xinyi Tu6Wootae Kim7Qin Zhou8Chao Zhang9Ping Yin10Kuntian Luo11Zhenkun Lou12Department of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo ClinicC-terminal binding protein (CtBP) interacting protein (CtIP) is a fundamental factor for the initiation of DNA end resection to initiate DNA repair. Here the authors reveal mechanistic insights into the regulation of CtIP via the deubiquitinase USP52.https://doi.org/10.1038/s41467-020-19202-0
spellingShingle Ming Gao
Guijie Guo
Jinzhou Huang
Jake A. Kloeber
Fei Zhao
Min Deng
Xinyi Tu
Wootae Kim
Qin Zhou
Chao Zhang
Ping Yin
Kuntian Luo
Zhenkun Lou
USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP
Nature Communications
title USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP
title_full USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP
title_fullStr USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP
title_full_unstemmed USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP
title_short USP52 regulates DNA end resection and chemosensitivity through removing inhibitory ubiquitination from CtIP
title_sort usp52 regulates dna end resection and chemosensitivity through removing inhibitory ubiquitination from ctip
url https://doi.org/10.1038/s41467-020-19202-0
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