|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2003-12-3
|
|
pubmed:abstractText |
The protein inhibitor of activated STAT1 (PIAS1), known to be a small ubiquitin-like modifier (SUMO) E3 ligase, was found to interact with the human cytomegalovirus IE2 protein. We found that the sumoylation of IE2 was markedly enhanced by wild-type PIAS1 but not by a mutant containing a Cys to Ser substitution at position 351 (C351S) within the RING finger-like domain. In target reporter gene assays, wild-type PIAS1, but not the C351S mutant, enhanced the IE2-mediated transactivations of viral polymerase promoter and cellular cyclin E promoter and this augmentation required the intact sumoylation sites of IE2. Our results suggest that PIAS1 acts as a SUMO E3 ligase toward IE2 and that it may regulate the transactivation function of IE2. To our knowledge, IE2 is the first viral target found to be regulated by a SUMO E3 ligase.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosidases,
http://linkedlifedata.com/resource/pubmed/chemical/IE2 protein, Cytomegalovirus,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Inhibitors of Activated STAT,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
4
|
|
pubmed:volume |
555
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
322-8
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:14644436-Amino Acid Substitution,
pubmed-meshheading:14644436-Animals,
pubmed-meshheading:14644436-Binding Sites,
pubmed-meshheading:14644436-Cell Line,
pubmed-meshheading:14644436-Cytomegalovirus,
pubmed-meshheading:14644436-DNA-Directed DNA Polymerase,
pubmed-meshheading:14644436-Galactosidases,
pubmed-meshheading:14644436-Genes, Reporter,
pubmed-meshheading:14644436-Humans,
pubmed-meshheading:14644436-Immediate-Early Proteins,
pubmed-meshheading:14644436-Promoter Regions, Genetic,
pubmed-meshheading:14644436-Protein Inhibitors of Activated STAT,
pubmed-meshheading:14644436-Protein Structure, Tertiary,
pubmed-meshheading:14644436-Proteins,
pubmed-meshheading:14644436-Recombinant Fusion Proteins,
pubmed-meshheading:14644436-SUMO-1 Protein,
pubmed-meshheading:14644436-Trans-Activators,
pubmed-meshheading:14644436-Transcriptional Activation,
pubmed-meshheading:14644436-Transfection,
pubmed-meshheading:14644436-Ubiquitin-Protein Ligases
|
|
pubmed:year |
2003
|
|
pubmed:articleTitle |
PIAS1 enhances SUMO-1 modification and the transactivation activity of the major immediate-early IE2 protein of human cytomegalovirus.
|
|
pubmed:affiliation |
Department of Molecular Cell Biology, Sungkyunkwan University, School of Medicine, Samsung Biomedical Research Institute, 300 Chunchundong, Jangangu, Kyonggido 440-746, South Korea.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
