Nuclear deubiquitination in the spotlight: the multifaceted nature of USP7 biology in disease

Radhika Rawat, Daniel T. Starczynowski, Panagiotis Ntziachristos

Research output: Contribution to journalReview articlepeer-review

12 Scopus citations


Ubiquitination is a versatile and tightly regulated post-translational protein modification with many distinct outcomes affecting protein stability, localization, interactions, and activity. Ubiquitin chain linkages anchored on substrates can be further modified by additional post-translational modifications, including phosphorylation and SUMOylation. Deubiquitinases (DUBs) reverse these ubiquitin marks with matched levels of precision. Over hundred known DUBs regulate a wide variety of cellular events. In this review, we focus on ubiquitin-specific protease 7 (USP7, also known as herpesvirus-associated ubiquitin-specific protease, or HAUSP) as one of the best studied, disease-associated DUBs. By highlighting the functions of USP7, particularly in the nucleus, and the emergence of the newest generation of USP7 inhibitors, we illustrate the importance of individual DUBs in the nucleus, and the therapeutic prospects of DUB targeting in human disease.

Original languageEnglish (US)
Pages (from-to)85-94
Number of pages10
JournalCurrent Opinion in Cell Biology
StatePublished - Jun 2019

ASJC Scopus subject areas

  • Cell Biology

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