Evidence map›Paper›PMID 23029315›Full record

ArticlePloS one2012

Lamin A/C mutants disturb sumo1 localization and sumoylation in vitro and in vivo.

Émilie Boudreau, Sarah Labib, Anne T Bertrand, Valérie Decostre, Pierrette M Bolongo, Nicolas Sylvius, Gisèle Bonne, Frédérique Tesson

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
1.2field-weighted citation impact, top 23% 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, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Frontiers in genetics · 2023
    Article
  4. Article
  5. Post-Translational Modification of Lamins: Mechanisms and Functions.Frontiers in cell and developmental biology · 2022
    Review
  6. Article
  7. Article
  8. Genotype-phenotype analysis of LMNA-related diseases predicts phenotype-selective alterations in lamin phosphorylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  9. Review
  10. Review
  11. Article
  12. Intermediate filaments and IF-associated proteins: from cell architecture to cell proliferation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  13. Article
  14. Article
  15. The Roles of SUMO in Metabolic Regulation.Advances in experimental medicine and biology · 2017
    Review
  16. Review
  17. Review
  18. Review
  19. Review
  20. Article
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

8 authors at 4 institutions in 2 countries.

Émilie BoudreauInterdisciplinary School of Health Sciences, University of Ottawa, Ottawa, Ontario, Canada.
Sarah Labib
Anne T Bertrand
Valérie Decostre
Pierrette M Bolongo
Nicolas Sylvius
Gisèle Bonne
Frédérique Tesson
University of Ottawa · CAFondation pour l’innovation en Cadiométabolisme et Nutrition · FRInserm · FRSorbonne Université · FR

Funding

Canadian Institutes of Health Research 77685
6 · The paper itself

Abstract

A-type lamins A and C are nuclear intermediate filament proteins in which mutations have been implicated in multiple disease phenotypes commonly known as laminopathies. A few studies have implicated sumoylation in the regulation of A-type lamins. Sumoylation is a post-translational protein modification that regulates a wide range of cellular processes through the attachment of small ubiquitin-related modifier (sumo) to various substrates. Here we showed that laminopathy mutants result in the mislocalization of sumo1 both in vitro (C2C12 cells overexpressing mutant lamins A and C) and in vivo (primary myoblasts and myopathic muscle tissue from the Lmna(H222P/H222P) mouse model). In C2C12 cells, we showed that the trapping of sumo1 in p.Asp192Gly, p.Gln353Lys, and p.Arg386Lys aggregates of lamin A/C correlated with an increased steady-state level of sumoylation. However, lamin A and C did not appear to be modified by sumo1. Our results suggest that mutant lamin A/C alters the dynamics of sumo1 and thus misregulation of sumoylation may be contributing to disease progression in laminopathies.

Indexed as

Mutation, MissenseProtein Processing, Post-TranslationalAnimalsCell LineChlorocebus aethiopsCOS CellsGene ExpressionLamin Type AMiceMice, TransgenicMuscle, SkeletalMuscular DiseasesMyoblasts, SkeletalPrimary Cell CultureProtein IsoformsProtein TransportLamin Type AProtein IsoformsSUMO-1 ProteinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID23029315
PMCPMC3448699
OpenAlexW1984185325

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.