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    J Cell Biochem. 2011 Dec;112(12):3856-62. doi: 10.1002/jcb.23317.

    USP7 regulates the stability and function of HLTF through deubiquitination.

    Qing P, Han L, Bin L, Yan L, Ping WX.

    Source

    Department of Respiratory Diseases, Minhang District Central Hospital, Shanghai, P.R. China.

    Abstract

    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.

    Copyright © 2011 Wiley Periodicals, Inc.

    PMID:
    21845734
    [PubMed - indexed for MEDLINE]

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