Viruses and the 26S proteasome: hacking into destruction.
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.
Banks
Lawrence
L
International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy. banks@icgeb.org
Pim
David
D
Thomas
Miranda
M
D000256:Adenoviridae / Q000378:metabolism; D000818:Animals; D006801:Humans; D017874:Immediate-Early Proteins / Q000502:physiology; D008025:Ligases / Q000737:chemistry; D008954:Models, Biological; D009856:Oncogene Proteins, Viral / Q000378:metabolism / Q000502:physiology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D012097:Repressor Proteins; D044767:Ubiquitin-Protein Ligases
C068651:E6 protein, Human papillomavirus type 16; D017874:Immediate-Early Proteins; D009856:Oncogene Proteins, Viral; D012097:Repressor Proteins; D044767:Ubiquitin-Protein Ligases; C051804:Vmw110 protein, Human herpesvirus 1; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; D008025:Ligases