Evidence map›Paper›PMID 21616059›Full record

ArticleBiochemical and biophysical research communications2011

Activity-dependent SUMOylation of the brain-specific scaffolding protein GISP.

Sriharsha Kantamneni, Kevin A Wilkinson, Nadia Jaafari, Emi Ashikaga, Daniel Rocca, Philip Rubin, Susan C Jacobs, Atsushi Nishimune, Jeremy M Henley

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. SUMOylation of Argonaute-2 regulates RNA interference activity.Biochemical and biophysical research communications · 2015
    Article
  6. Review
  7. Review
  8. Article
  9. In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  10. Article
  11. Protein SUMOylation in spine structure and function.Current opinion in neurobiology · 2012
    Review
  12. Article
  13. Enhanced SUMOylation and SENP-1 protein levels following oxygen and glucose deprivation in neurones.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2012
    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

9 authors at 2 institutions in 2 countries.

Sriharsha KantamneniMRC Centre for Synaptic Plasticity, School of Biochemistry, Medical Sciences Building, University of Bristol, Bristol BS8 1TD, UK.
Kevin A Wilkinson
Nadia Jaafari
Emi Ashikaga
Daniel Rocca
Philip Rubin
Susan C Jacobs
Atsushi Nishimune
Jeremy M Henley
University of Bristol · GBUniversity of Fukui · JP

Funding

Medical Research Council G0601810Wellcome Trust 074017Wellcome Trust 083721
6 · The paper itself

Abstract

G-protein coupled receptor interacting scaffold protein (GISP) is a multi-domain, brain-specific protein derived from the A-kinase anchoring protein (AKAP)-9 gene. Using yeast two-hybrid screens to identify GISP interacting proteins we isolated the SUMO conjugating enzyme Ubc9. GISP interacts with Ubc9 in vitro, in heterologous cells and in neurons. SUMOylation is a post-translational modification in which the small protein SUMO is covalently conjugated to target proteins, modulating their function. Consistent with its interaction with Ubc9, we show that GISP is SUMOylated by both SUMO-1 and SUMO-2 in both in vitro SUMOylation assays and in mammalian cells. Intriguingly, SUMOylation of GISP in neurons occurs in an activity-dependent manner in response to chemical LTP. These data suggest that GISP is a novel neuronal SUMO substrate whose SUMOylation status is modulated by neuronal activity.

Indexed as

SumoylationA Kinase Anchor ProteinsAnimalsBrainChlorocebus aethiopsCOS CellsCytoskeletal ProteinsNerve Tissue ProteinsNeuronsRatsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinTwo-Hybrid System TechniquesUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Akap9 protein, ratA Kinase Anchor ProteinsCytoskeletal ProteinsNerve Tissue ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, ratUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID21616059
PMCPMC3308138
OpenAlexW2077318935

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.