Literature DB >> 16275358

Functional annotation of deubiquitinating enzymes using RNA interference.

Annette M G Dirac1, Sebastian M B Nijman, Thijn R Brummelkamp, René Bernards.   

Abstract

Protein ubiquitination is a dynamic process, depending on a tightly regulated balance between the activity of ubiquitin ligases and their antagonists, the ubiquitin-specific proteases or deubiquitinating enzymes. The family of ubiquitin ligases has been studied intensively and it is well established that their deregulation contributes to diverse disease processes, including cancer. Much less is known about the function and regulation of the large group of deubiquitinating enzymes. This chapter describes how RNA interference against deubiquitinating enzymes can be used to elucidate their function. The application of this technology will greatly improve the functional annotation of this family of proteases.

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Year:  2005        PMID: 16275358     DOI: 10.1016/S0076-6879(05)98045-2

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  3 in total

1.  The ubiquitin-specific protease 12 (USP12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation.

Authors:  Julien Moretti; Patricia Chastagner; Chih-Chao Liang; Martin A Cohn; Alain Israël; Christel Brou
Journal:  J Biol Chem       Date:  2012-07-09       Impact factor: 5.157

2.  The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation.

Authors:  Julien Moretti; Patricia Chastagner; Stefano Gastaldello; Sara F Heuss; Annette M Dirac; René Bernards; Maria G Masucci; Alain Israël; Christel Brou
Journal:  PLoS Biol       Date:  2010-11-23       Impact factor: 8.029

3.  Monitoring Target Engagement of Deubiquitylating Enzymes Using Activity Probes: Past, Present, and Future.

Authors:  Jeanine Harrigan; Xavier Jacq
Journal:  Methods Mol Biol       Date:  2016
  3 in total

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