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Trends Biochem Sci. 2003 Aug;28(8):452-9.

Viruses and the 26S proteasome: hacking into destruction.

Author information

1
International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy. banks@icgeb.org

Abstract

The discovery that the human papillomavirus E6 oncoprotein could direct the ubiquitination and degradation of the p53 tumour suppressor at the 26S proteasome was the beginning of a new view on virus-host interactions. A decade later, a plethora of viral proteins have been shown to direct host-cell proteins for proteolytic degradation. These activities are required for various aspects of the virus life-cycle from entry, through replication and enhanced cell survival, to viral release. As with oncogenes and cell-cycle control, the study of apparently simple viruses has provided a wealth of information on the function of a whole class of cellular proteins whose function is arguably as important as that of the kinases: the ubiquitin-protein ligases.

PMID:
12932734
DOI:
10.1016/S0968-0004(03)00141-5
[Indexed for MEDLINE]

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