Evidence map›Paper›PMID 27623146›Full record

ArticleeLife2016

A model for regulation by SynGAP-α1 of binding of synaptic proteins to PDZ-domain 'Slots' in the postsynaptic density.

Ward G Walkup, Tara L Mastro, Leslie T Schenker, Jost Vielmetter, Rebecca Hu, Ariella Iancu, Meera Reghunathan, Barry Dylan Bannon, Mary B Kennedy

Erratum issuedAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
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

60 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Dissociation of SYNGAP1 enzymatic and structural roles: Intrinsic excitability and seizure susceptibility.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. A spatial model of autophosphorylation of CabioRxiv : the preprint server for biology · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Context-dependent hyperactivity inFrontiers in molecular neuroscience · 2024
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Ward G WalkupDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Tara L MastroDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Leslie T SchenkerDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Jost VielmetterBeckman Institute Protein Expression Center, California Institute of Technology, Pasadena, United States.
Rebecca HuDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Ariella IancuDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Meera ReghunathanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Barry Dylan BannonDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Mary B KennedyDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0003-1369-0525

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
Binding of synGAP to PDZ domains of PSD-95 and its role in Intellectual Disability and Autism Spectrum Disorders caused by synGAP haploinsufficiencyR01MH115456 · NIMH · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI KENNEDY, MARY B · 2018 to 2021
$1.7M
Time Resolved Assay of Synaptic Enzyme Activity by Mass SpectrometryR01MH095095 · NIMH · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI KENNEDY, MARY B · 2011 to 2014
$1.7M
NIGMS NIH HHS T32 GM007616NIMH NIH HHS R01 MH095095NIMH NIH HHS R01 MH115456
6 · The paper itself

Abstract

SynGAP is a Ras/Rap GTPase-activating protein (GAP) that is a major constituent of postsynaptic densities (PSDs) from mammalian forebrain. Its α1 isoform binds to all three PDZ (PSD-95, Discs-large, ZO-1) domains of PSD-95, the principal PSD scaffold, and can occupy as many as 15% of these PDZ domains. We present evidence that synGAP-α1 regulates the composition of the PSD by restricting binding to the PDZ domains of PSD-95. We show that phosphorylation by Ca

Indexed as

PDZ DomainsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Disks Large Homolog 4 ProteinMicePhosphorylationPost-Synaptic DensityProtein Processing, Post-TranslationalProtein Serine-Threonine Kinasesras GTPase-Activating ProteinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Disks Large Homolog 4 ProteinProtein Serine-Threonine Kinasesras GTPase-Activating Proteinsserum-inducible kinaseSyngap1 protein, mousebiochemistryCaMKIImouseneurosciencesynaptic plasticitySynGAP haploinsufficiency

Identifiers

PMID27623146
PMCPMC5040590

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.