Evidence map›Paper›PMID 23684609›Full record

ArticleCell reports2013

Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo.

Prashant Sharma, Satoru Yamada, Margaret Lualdi, Mary Dasso, Michael R Kuehn

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. SUMO Antibody Validation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  4. Review
  5. Review
  6. Protein sumoylation in normal and cancer stem cells.Frontiers in molecular biosciences · 2022
    Review
  7. Article
  8. Regulation of Serotonin 1A Receptor SUMOylation by SENP2 and PIASxα.International journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
  12. Article
  13. Review
  14. Observational
  15. Article
  16. Article
  17. SUMO protease SENP1 deSUMOylates and stabilizes c-Myc.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Quantitative high-throughput screening identifies cytoprotective molecules that enhance SUMO conjugation via the inhibition of SUMO-specific protease (SENP)2.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  19. SUMOylation in brain ischemia: Patterns, targets, and translational implications.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2018
    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

5 authors at 5 institutions in 2 countries.

Prashant SharmaLaboratory of Protein Dynamics and Signaling, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Satoru Yamada
Margaret Lualdi
Mary Dasso
Michael R Kuehn
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Cancer Institute · USNational Institutes of Health · USOsaka University · JPScience Applications International Corporation (United States) · US

Funding

SUMO family Ubiquitin-like Modifiers In Higher EukaryotesZIAHD001902 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DASSO, MARY C. · 2009 to 2021
$6.3M
Ubiquitin And SUMO Post-Translational Modifications In Development And DiseaseZIABC009297 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI KUEHN, MICHAEL · 2009 to 2013
$2.8M
Intramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA BC009297NCI NIH HHS Y99 CA999999
6 · The paper itself

Abstract

Posttranslational modification with small ubiquitin-like modifier (Sumo) regulates numerous cellular and developmental processes. Sumoylation is dynamic with deconjugation by Sumo-specific proteases (Senps) regulating steady-state levels. Different Senps are found in distinct subcellular domains, which may limit their deconjugation activity to colocalizing Sumo-modified proteins. In vitro, Senps can discriminate between the different Sumo paralogs: Sumo1 versus the highly related Sumo2 and Sumo3 (Sumo2/3), which can form poly-Sumo chains. However, a full understanding of Senp specificity in vivo is still lacking. Here, using biochemical and genetic approaches, we establish that Senp1 has an essential, nonredundant function to desumoylate Sumo1-modified proteins during mouse embryonic development. Senp1 specificity for Sumo1 conjugates represents an intrinsic function and not simply a product of colocalization. In contrast, Senp1 has only a limited role in Sumo2/3 desumoylation, although it may regulate Sumo1-mediated termination of poly-Sumo2/3 chains.

Indexed as

AllelesAnimalsCells, CulturedCysteine EndopeptidasesEmbryo, MammalianEmbryonic DevelopmentEmbryonic Stem CellsEndopeptidasesHEK293 CellsHeterozygoteHumansMiceMutationPhenotypeSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinCysteine EndopeptidasesEndopeptidasesSenp1 protein, mouseSenp2 protein, mouseSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, mouseSumo3 protein, mouseUbiquitins

Identifiers

PMID23684609
PMCPMC3775507
OpenAlexW2022249676

What OpenQuestion holds

Textmetadata
LicenceTDM
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.