✦ LIBER ✦

USP7 regulates the stability and function of HLTF through deubiquitination

✍ Scribed by Peng Qing; Lu Han; Liu Bin; Lu Yan; Wen Xue Ping

Book ID: 102301189
Publisher: John Wiley and Sons
Year: 2011
Tongue: English
Weight: 363 KB
Volume: 112
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.23317

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✦ Synopsis

Human helicase-like transcription factor (HLTF) is a functional homologue of yeast Rad5 that regulates error-free replication through DNA lesions. HLTF promotes the Lys-63-linked polyubiquitination of proliferating cell nuclear antigen (PCNA) that is required for maintaining genomic stability. Here, we identified the deubiquitylating enzyme ubiquitin-specific protease 7 (USP7) as a novel regulator of HLTF stability. We found that USP7 interacted with and stabilized HLTF after genotoxic stress. Furthermore, USP7 mediated deubiquitination significantly prolonged the half-life of HLTF, which in turn increased PCNA polyubiquitination. More intriguingly, silencing of USP7 rendered A549 cells highly sensitive to DNA damage and over-expression of HLTF attenuated this sensitivity. Thus, our results delineate a previously unknown USP7-HLTF-PCNA molecular network controlling DNA damage response.

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