Source:http://linkedlifedata.com/resource/pubmed/id/12466471
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 12
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pubmed:dateCreated |
2002-12-5
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pubmed:abstractText |
Early during infection, the herpes simplex regulatory protein ICP0 promotes the proteasome-dependent degradation of a number of cellular proteins and the loss of a number of SUMO-1-modified protein isoforms, including PML. Recently, ICP0 has been shown to induce the accumulation of conjugated ubiquitin and function as a ubiquitin E3 ligase. However, certain aspects of the biochemistry, cell biology and the links between SUMO-1 conjugation/deconjugation and protein degradation remain unclear. For example, it is not currently known whether SUMO-1 deconjugation is a prerequisite for ubiquitination or degradation and, if so, by what mechanism this may occur. To help address these questions, a SUMO-specific protease (SENP1) was cloned and its expression and localization in relation to ICP0 examined. A cell line was established which constitutively expresses SUMO-1 to facilitate studies of localization and biochemistry. SENP1 localized to the nucleus mainly in discrete subdomains, a subset of which co-localized with the PML bodies. Both ICP0 and SENP1 protease promoted the loss of SUMO-1 from the nucleus, observed both for the endogenous species and the cell line expressing the epitope-tagged SUMO-1. The tagged SUMO-1 was recruited into high molecular mass conjugates in the cell line, and expression of SENP1 promoted loss of these species, including the modified species of PML. Finally, in co-transfection experiments ICP0 promoted the recruitment of SENP1 to nuclear domains, a result which was also observed early during infection. The significance of these findings is discussed in relation to the function of ICP0.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SENP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Vmw110 protein, Human herpesvirus 1
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2951-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12466471-Amino Acid Sequence,
pubmed-meshheading:12466471-Animals,
pubmed-meshheading:12466471-Cell Line,
pubmed-meshheading:12466471-Cell Nucleus Structures,
pubmed-meshheading:12466471-Cercopithecus aethiops,
pubmed-meshheading:12466471-Endopeptidases,
pubmed-meshheading:12466471-HeLa Cells,
pubmed-meshheading:12466471-Herpesvirus 1, Human,
pubmed-meshheading:12466471-Humans,
pubmed-meshheading:12466471-Immediate-Early Proteins,
pubmed-meshheading:12466471-Molecular Sequence Data,
pubmed-meshheading:12466471-SUMO-1 Protein,
pubmed-meshheading:12466471-Sequence Analysis, DNA,
pubmed-meshheading:12466471-Transfection,
pubmed-meshheading:12466471-Ubiquitin-Protein Ligases,
pubmed-meshheading:12466471-Vero Cells
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pubmed:year |
2002
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pubmed:articleTitle |
Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease.
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pubmed:affiliation |
Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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