Ubiquitin-specific Peptidase 42 (USP42) functions to deubiquitylate histones and regulate transcriptional activity

Hock, A. K., Vigneron, A. M. and Vousden, K. H. (2014) Ubiquitin-specific Peptidase 42 (USP42) functions to deubiquitylate histones and regulate transcriptional activity. Journal of Biological Chemistry, 289(50), pp. 34862-34870. (doi: 10.1074/jbc.M114.589267)

Abstract

Ubiquitin-specific peptidase 42 (USP42) is a deubiquitylating enzyme that can target p53 and contribute to the stabilization of p53 in response to stress. We now show that USP42 can also regulate transcription independently of p53. USP42 co-localized with RNA polymerase II (RNA Pol II) in nuclear foci, bound to histone H2B, and deubiquitylated H2B. Depletion of USP42 increased H2B ubiquitylation at a model promoter and decreased both basal and induced transcription from a number of promoters. These results are consistent with a role for USP42 in regulating transcription by deubiquitylating histones.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Hock, Dr Andreas and Vigneron, Dr Arnaud and Vousden, Karen
• Authors: Hock, A. K., Vigneron, A. M., and Vousden, K. H.
• College/School: College of Medical Veterinary and Life Sciences > School of Cancer Sciences
• Journal Name: Journal of Biological Chemistry
• Publisher: American Society for Biochemistry and Molecular Biology, Inc.
• ISSN: 0021-9258
• ISSN (Online): 1083-351X
• Copyright Holders: Copyright © 2014 The American Society for Biochemistry and Molecular Biology, Inc.
• First Published: First published in the Journal of Biological Chemistry 289(50):34862-34870
• Publisher Policy: Reproduced under a Creative Commons License