Evidence map›Paper›PMID 20382164›Full record

ArticleJournal of molecular biology2010

SUMOylation of the lens epithelium-derived growth factor/p75 attenuates its transcriptional activity on the heat shock protein 27 promoter.

Murilo T D Bueno, Jose A Garcia-Rivera, Jeffrey R Kugelman, Elisa Morales, Germán Rosas-Acosta, Manuel Llano

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Murilo T D BuenoDepartment of Biological Sciences, University of Texas at El Paso, 500 West University Avenue, El Paso, TX 79968, USA.
Jose A Garcia-Rivera
Jeffrey R Kugelman
Elisa Morales
Germán Rosas-Acosta
Manuel Llano
The University of Texas at El Paso · US

Funding

TOXICOLOGY PROJECTG12RR008124 · NCRR · UNIVERSITY OF TEXAS EL PASO · PI WALSH, ELIZABETH J · 1992 to 2011
$20.8M
RISE Scholars Program at UTEPR25GM069621 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI AGUILERA, RENATO J · 2004 to 2021
$11.2M
Molecular Mechanism of LEDGF/p75 in HIV IntegrationSC2GM082301 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI LLANO, MANUEL · 2008 to 2010
$407k
The Sumoylation System as a Novel Target for Anti-Influenza TherapiesSC2AI081377 · NIAID · UNIVERSITY OF TEXAS EL PASO · PI ROSAS-ACOSTA, GERMAN · 2008 to 2010
$332k
Howard Hughes Medical Institute 52005908NCRR NIH HHS 5G12RR008124NCRR NIH HHS G12 RR008124NIAID NIH HHS 1SC2AI081377-01NIAID NIH HHS SC2 AI081377NIGMS NIH HHS 1SC2GM082301-01NIGMS NIH HHS 2R25GM069621-05NIGMS NIH HHS R25 GM069621NIGMS NIH HHS SC2 GM082301
6 · The paper itself

Abstract

Lens epithelium-derived growth factor (LEDGF) proteins p75 and p52 are transcriptional coactivators that connect sequence-specific activators to the basal transcription machinery. We have found that these proteins are posttranslationally modified by SUMO (small ubiquitin-like modifier)-1 and SUMO-3. Three SUMOylation sites, K75, K250, and K254, were mapped on the shared N-terminal region of these molecules, while a fourth site, K364, was identified in the C-terminal part exclusive of LEDGF/p75. The N-terminal SUMO targets are located in evolutionarily conserved charge-rich regions that lack resemblance to the described consensus SUMOylation motif, whereas the C-terminal SUMO target is solvent exposed and situated in a typical consensus motif. SUMOylation did not affect the cellular localization of LEDGF proteins and was not necessary for their chromatin-binding ability, nor did it affect this activity. However, lysine to arginine mutations of the identified SUMO acceptor sites drastically inhibited LEDGF SUMOylation, extended the half-life of LEDGF/p75, and significantly increased its transcriptional activity on the heat shock protein 27 promoter, indicating a negative effect of SUMOylation on the transcriptional activity of LEDGF/p75. Considering that SUMOylation is known to negatively affect the transcriptional activity of all transcription factors known to transactivate heat shock protein 27 expression, these findings support the paradigm establishing SUMOylation as a global neutralizer of cellular processes upregulated upon cellular stress.

Indexed as

Promoter Regions, GeneticTranscriptional ActivationAmino Acid SubstitutionCell LineHalf-LifeHSP27 Heat-Shock ProteinsHumansIntercellular Signaling Peptides and ProteinsMutagenesis, Site-DirectedProtein Processing, Post-TranslationalSUMO-1 ProteinTranscription FactorsUbiquitinsHSP27 Heat-Shock ProteinsIntercellular Signaling Peptides and Proteinslens epithelium-derived growth factorSUMO-1 ProteinSUMO3 protein, humanTranscription FactorsUbiquitins

Identifiers

PMID20382164
PMCPMC2875294
OpenAlexW2001366457

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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.