Journal article
SUMO-1 Modification of Human Cytomegalovirus IE1/IE72
Journal of virology, v 76(6), pp 2990-2996
Mar 2002
PMID: 11861864
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Human cytomegalovirus (HCMV) immediate-early protein IE1/IE72 is involved in undermining many cellular processes including cell cycle regulation, apoptosis, nuclear architecture, and gene expression. The multifunctional nature of IE72 suggests that posttranslational modifications may modulate its activities. IE72 is a phosphoprotein and has intrinsic kinase activity (S. Pajovic, E. L. Wong, A. R. Black, and J. C. Azizkhan, Mol. Cell. Biol. 17:6459-6464, 1997). We now demonstrate that IE72 is covalently conjugated to the small ubiquitin-like modifier (SUMO-1). SUMO-1 is an 11.5-kDa protein that is conjugated to multiple proteins and has been reported to exhibit multiple effects, including modulation of protein stability, subcellular localization, and gene expression. A covalently modified protein migrating at ∼92 kDa, which is stabilized by a SUMO-1 hydrolase inhibitor, is revealed by Western blotting with anti-IE72 of lysates from cells infected with HCMV or cells expressing IE72. SUMO modification of IE72 was confirmed by immunoprecipitation with anti-IE72 and anti-SUMO-1 followed by Western blotting with anti-SUMO-1 and anti-IE72, respectively. Lysine 450 is within a sumoylation consensus site (I,V,L)KXE; changing lysine 450 to arginine by point mutation abolishes SUMO-1 modification of IE72. Inhibition of protein phosphatase 1 and 2A, which increases the phosphorylation of IE72, suppresses the formation of SUMO-1-IE72 conjugates. Both wild-type IE72 and IE72
K450R
localize to nuclear PML oncogenic domains and disrupt them. Studies of protein stability, transactivation, and complementation of IE72-deficient HCMV (CR208) have revealed no significant differences between wild-type IE72 and IE72
K450R
.
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Details
- Title
- SUMO-1 Modification of Human Cytomegalovirus IE1/IE72
- Creators
- Mary L Spengler - Department of Pharmacology and Therapeutics, Roswell Park Cancer Institute, Buffalo, New YorkKaren Kurapatwinski - Department of Pharmacology and Therapeutics, Roswell Park Cancer Institute, Buffalo, New YorkAdrian R Black - Department of Pharmacology and Therapeutics, Roswell Park Cancer Institute, Buffalo, New YorkJane Azizkhan-Clifford - Department of Pharmacology and Therapeutics, Roswell Park Cancer Institute, Buffalo, New York
- Publication Details
- Journal of virology, v 76(6), pp 2990-2996
- Publisher
- American Society for Microbiology
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000174039400041
- Scopus ID
- 2-s2.0-0036184785
- Other Identifier
- 991014877805904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Virology