Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Herpesvirus-Associated Ubiquitin-Specific Protease De-ubiquitinase

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_2690-2

Synonyms

Definition

The cysteine protease de-ubiquitinase (DUB) herpesvirus-associated ubiquitin-specific protease (HAUSP) has been fairly well characterized in recent years and has emerged as an important component of the p53-Mdm2 signaling pathway.

Characteristics

De-ubiquitinases are specific protease enzymes that catalyze the removal of ubiquitin from substrates by cleaving the isopeptide bond between ubiquitin and substrate. The de-ubiquitination enzyme family (DUBs) falls within two classes of proteases: the metalloproteases and cysteine proteases, though most DUBs fall within the latter. Further classification subdivides the cysteine proteases into four subclasses: ubiquitin C-terminal hydrolases (UCH), ubiquitin-specific proteases (USP), Machado-Joseph disease proteases (MJD), and Otubain proteases (OTU). The MJD and OTU subclasses were more recently identified through a bioinformatics approach. MJD is a rare hereditary...

Keywords

Cysteine Protease Mdm2 Protein Cancer Cell Line HCT116 Colorectal Cancer Cell Line HCT116 Rare Hereditary Disorder 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in to check access.

References

  1. Brooks CL, Gu W (2003) Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr Opin Cell Biol 15:164–171CrossRefPubMedGoogle Scholar
  2. Li M, Chen D, Shiloh A et al (2002) Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416:648–653CrossRefPubMedGoogle Scholar
  3. Li M, Brooks CL, Kon N et al (2004) A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 13:879–886CrossRefPubMedGoogle Scholar
  4. Nijman SMB, Luna-Vargas MPA, Velds A et al (2005) A genomic and functional inventory of deubiquitinating enzymes. Cell 123:773–786CrossRefPubMedGoogle Scholar
  5. Vogelstein B, Lane D, Levine AJ (2000) Surfing the p53 network. Nature 408:307–310CrossRefPubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Institute for Cancer Genetics, and Department of PathologyCollege of Physicians and Surgeons, Columbia UniversityNew YorkUSA