Evidence map›Paper›PMID 20424159›Full record

ArticleThe Journal of biological chemistry2010

Rhes, a physiologic regulator of sumoylation, enhances cross-sumoylation between the basic sumoylation enzymes E1 and Ubc9.

Srinivasa Subramaniam, Robert G Mealer, Katherine M Sixt, Roxanne K Barrow, Alessandro Usiello, Solomon H Snyder

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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. SUMO-modifying Huntington's disease.IBRO neuroscience reports · 2022
    Review
  10. Article
  11. Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022
    Review
  12. Deletion of SUMO1 attenuates behavioral and anatomical deficits by regulating autophagic activities in Huntington disease.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Rhes Tunnels: A Radical New Way of Communication in the Brain's Striatum?BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Review
  18. Review
  19. Article
  20. Rhes, a striatal-enriched protein, promotes mitophagy via Nix.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

6 authors at 3 institutions in 2 countries.

Srinivasa SubramaniamSolomon H. Snyder Department of Neuroscience, Departments of Pharmacology and Molecular Sciences and Psychiatry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Robert G Mealer
Katherine M Sixt
Roxanne K Barrow
Alessandro Usiello
Solomon H Snyder
Johns Hopkins Medicine · USJohns Hopkins University · USCeinge Biotecnologie Avanzate (Italy) · IT

Funding

NEUROCHEMICAL ACTIONS OF PSYCHOTROPIC DRUGSR37MH018501 · NIMH · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1990 to 2009
$11.5M
NEUROCHEMICAL ACTIONS OF PSYCHOTROPIC DRUGSR01MH018501 · NIMH · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2019
$10.8M
NEUROTRANSMITTER RECEPTORSK05DA000074 · NIDA · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2009
$1.3M
NIDA NIH HHS DA00074NIDA NIH HHS K05 DA000074NIMH NIH HHS MH18501NIMH NIH HHS R01 MH018501NIMH NIH HHS R37 MH018501
6 · The paper itself

Abstract

We recently reported that the small G-protein Rhes has the properties of a SUMO-E3 ligase and mediates mutant huntingtin (mHtt) cytotoxicity. We now demonstrate that Rhes is a physiologic regulator of sumoylation, which is markedly reduced in the corpus striatum of Rhes-deleted mice. Sumoylation involves activation and transfer of small ubiquitin-like modifier (SUMO) from the thioester of E1 to the thioester of Ubc9 (E2) and final transfer to lysines on target proteins, which is enhanced by E3s. We show that E1 transfers SUMO from its thioester directly to lysine residues on Ubc9, forming isopeptide linkages. Conversely, sumoylation on E1 requires transfer of SUMO from the thioester of Ubc9. Thus, the process regarded as "autosumoylation" reflects intermolecular transfer between E1 and Ubc9, which we designate "cross-sumoylation." Rhes binds directly to both E1 and Ubc9, enhancing cross-sumoylation as well as thioester transfer from E1 to Ubc9.

Indexed as

AnimalsCorpus StriatumCysteineGlutamineGTP-Binding ProteinsHumansHuntington DiseaseLysineMiceMice, KnockoutMutationSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein LigasesCysteineGlutamineGTP-Binding ProteinsLysineRasd2 protein, mouseSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein Ligases

Identifiers

PMID20424159
PMCPMC2898300
OpenAlexW2145069182

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.