Evidence map›Paper›PMID 29773808›Full record

ArticleScientific reports2018

Quantitative SUMO proteomics reveals the modulation of several PML nuclear body associated proteins and an anti-senescence function of UBC9.

Francis P McManus, Véronique Bourdeau, Mariana Acevedo, Stéphane Lopes-Paciencia, Lian Mignacca, Frédéric Lamoliatte, John W Rojas Pino, Gerardo Ferbeyre, Pierre Thibault

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

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  20. [Involvement of PML proteins in treatment of acute promyelocytic leukemia with arsenic trioxide].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2018
    Review
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.

Francis P McManusInstitute of Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Véronique BourdeauDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Mariana AcevedoDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Stéphane Lopes-PacienciaDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Lian MignaccaDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Frédéric LamoliatteInstitute of Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3C 3J7, Canada.
John W Rojas PinoDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Gerardo FerbeyreDepartment of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, QC H3C 3J7, Canada. g.ferbeyre@umontreal.ca.
Pierre ThibaultInstitute of Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3C 3J7, Canada. pierre.thibault@umontreal.ca.
Université de Montréal · CAInstitute for Research in Immunology and Cancer · CA

Funding

CIHR RN196161-300726
6 · The paper itself

Abstract

Several regulators of SUMOylation have been previously linked to senescence but most targets of this modification in senescent cells remain unidentified. Using a two-step purification of a modified SUMO3, we profiled the SUMO proteome of senescent cells in a site-specific manner. We identified 25 SUMO sites on 23 proteins that were significantly regulated during senescence. Of note, most of these proteins were PML nuclear body (PML-NB) associated, which correlates with the increased number and size of PML-NBs observed in senescent cells. Interestingly, the sole SUMO E2 enzyme, UBC9, was more SUMOylated during senescence on its Lys-49. Functional studies of a UBC9 mutant at Lys-49 showed a decreased association to PML-NBs and the loss of UBC9's ability to delay senescence. We thus propose both pro- and anti-senescence functions of protein SUMOylation.

Indexed as

Cellular SenescenceCell NucleusHumansNuclear ProteinsPromyelocytic Leukemia ProteinProtein ConformationProteomeSmall Ubiquitin-Related Modifier ProteinsSumoylationTumor Cells, CulturedUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Nuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinProteomeSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID29773808
PMCPMC5958138
OpenAlexW2805922232

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.