Document Detail

Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific.
MedLine Citation:
PMID:  20034935     Owner:  NLM     Status:  MEDLINE    
Sumoylation has emerged as a major post-translational modification of cellular proteins, affecting a variety of cellular processes. Viruses have exploited the sumoylation pathway to advance their own replication by evolving several ways to perturb the host sumoylation apparatus. However, there has been no report of virally encoded enzymes directly involved in catalyzing the sumoylation reaction. Here, we report that the K-bZIP protein encoded by Kaposi's sarcoma-associated herpesvirus (KSHV) is a SUMO E3 ligase with specificity toward SUMO2/3. K-bZIP is a nuclear factor that functions to modulate viral gene expression and to prolong the G1 phase, allowing viral transcription and translation to proceed at the early stage of infection. In addition to functioning as a transcriptional factor, we show that K-bZIP carries a SIM (SUMO-interacting motif), which specifically binds to SUMO-2/3 but not SUMO-1. K-bZIP catalyzes its own SUMO modification as well as that of its interacting partners such as the cellular tumor suppressor proteins p53 and Rb, both in vitro and in vivo. This reaction depends on an intact SIM. Sumoylation of p53 leads to its activation and K-bZIP is recruited to several p53 target chromatin sites in a SIM-dependent manner. In addition to the identification of a viral SUMO-2/3 E3 ligase, our results provide additional insights into the mechanisms whereby K-bZIP induces cell cycle arrest.
Pei-Ching Chang; Yoshihiro Izumiya; Chun-Yi Wu; Latricia D Fitzgerald; Mel Campbell; Thomas J Ellison; Kit S Lam; Paul A Luciw; Hsing-Jien Kung
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2009-12-24
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-15     Completed Date:  2010-03-11     Revised Date:  2011-07-25    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5266-73     Citation Subset:  IM    
Department of Biological Chemistry and Molecular Medicine, University of California, Davis, California 95616, USA.
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MeSH Terms
Amino Acid Motifs / physiology
Basic-Leucine Zipper Transcription Factors / genetics,  metabolism*
Cell Line
G1 Phase / genetics
Gene Expression Regulation, Viral / physiology
Herpesvirus 8, Human / enzymology*,  genetics
Protein Processing, Post-Translational / genetics
Repressor Proteins / genetics,  metabolism*
Retinoblastoma Protein / genetics,  metabolism
Small Ubiquitin-Related Modifier Proteins / genetics,  metabolism*
Substrate Specificity / physiology
Tumor Suppressor Protein p53 / genetics,  metabolism
Ubiquitin-Protein Ligases / genetics,  metabolism*
Ubiquitins / genetics,  metabolism*
Viral Proteins / genetics,  metabolism*
Grant Support
Reg. No./Substance:
0/Basic-Leucine Zipper Transcription Factors; 0/K8 protein, Human herpesvirus 8; 0/Repressor Proteins; 0/Retinoblastoma Protein; 0/SUMO2 protein, human; 0/SUMO3 protein, human; 0/Small Ubiquitin-Related Modifier Proteins; 0/TP53 protein, human; 0/Tumor Suppressor Protein p53; 0/Ubiquitins; 0/Viral Proteins; EC Ligases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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