Evidence map›Paper›PMID 20034935›Full record

ArticleThe Journal of biological chemistry2010

Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific.

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

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.0field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 89 citations in OpenAlex.

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6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Pei-Ching ChangDepartment of Biological Chemistry and Molecular Medicine, University of California, Davis, California 95616, USA.
Yoshihiro Izumiya
Chun-Yi Wu
Latricia D Fitzgerald
Mel Campbell
Thomas J Ellison
Kit S Lam
Paul A Luciw
Hsing-Jien Kung
UC Davis Comprehensive Cancer CenterUniversity of California, Davis · US

Funding

ORF36 Viral Kinase as a Transcriptional Regulator of KSHVP01DE019085 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SUN, REN · 2008 to 2012
$6.4M
Androgen signaling and kinase regulation in PCAR01CA114575 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI KUNG, HSING-JIEN · 2005 to 2009
$1.3M
NCI NIH HHS R01 CA114575NIDCR NIH HHS DE019085NIDCR NIH HHS P01 DE019085
6 · The paper itself

Abstract

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.

Indexed as

Amino Acid MotifsBasic-Leucine Zipper Transcription FactorsCell LineG1 PhaseGene Expression Regulation, ViralHerpesvirus 8, HumanHumansProtein Processing, Post-TranslationalRepressor ProteinsRetinoblastoma ProteinSmall Ubiquitin-Related Modifier ProteinsSubstrate SpecificityTumor Suppressor Protein p53Ubiquitin-Protein LigasesUbiquitinsViral ProteinsBasic-Leucine Zipper Transcription FactorsK8 protein, Human herpesvirus 8Repressor ProteinsRetinoblastoma ProteinSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanTP53 protein, humanTumor Suppressor Protein p53Ubiquitin-Protein LigasesUbiquitinsViral Proteins

Identifiers

PMID20034935
PMCPMC2820755
OpenAlexW2053216715

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.