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Oncogene. 1999 Jan 28;18(4):935-41.

Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins.

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1
Centre National de la Recherche Scientifique Unité Propre de Recherche 9051, Laboratoire associé au Comité de Paris de la Ligue Contre le Cancer, Institut Universitaire d'Hématologie de l'université de Paris VII, France.

Abstract

The PML protein is associated to nuclear bodies (NBs) whose functions are as yet unknown. PML and two other NBs-associated proteins, Sp100 And ISG20 are directly induced by interferons (IFN). PML and Sp100 proteins are covalently linked to SUMO-1, and ubiquitin-like peptide. PML NBs are disorganized in acute promyelocytic leukemia and during several DNA virus infections. In particular, the HSV-1 ICP0 protein is known to delocalize PML from NBs. Thus, NBs could play an important role in oncogenesis, IFN response and viral infections. Here, we show that HSV-1 induced PML protein degradation without altering its mRNA level. This degradation was time- and multiplicity of infection-dependent. Sp100 protein was also degraded, while another SUMO-1 conjugated protein, RanGAP1 and the IFN-induced protein kinase PKR were not. The proteasome inhibitor MG132 abrogated the HSV-1-induced PML and Sp100 degradation and partially restored their NB-localization. HSV-1 induced PML and Sp100 degradation constitutes a new example of viral inactivation of IFN target gene products.

PMID:
10023669
DOI:
10.1038/sj.onc.1202366
[Indexed for MEDLINE]
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