Evidence map›Paper›PMID 25555912›Full record

ArticleThe Journal of biological chemistry2015

Subunit-specific regulation of N-methyl-D-aspartate (NMDA) receptor trafficking by SAP102 protein splice variants.

Zhe Wei, Blake Behrman, Wei-Hua Wu, Bo-Shiun Chen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Frontiers in molecular neuroscience · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. 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

4 authors at 1 institution in 1 country.

Zhe WeiFrom the Department of Neuroscience and Regenerative Medicine and Department of Neurology, Medical College of Georgia, Georgia Regents University, Augusta, Georgia 30912.
Blake BehrmanFrom the Department of Neuroscience and Regenerative Medicine and Department of Neurology, Medical College of Georgia, Georgia Regents University, Augusta, Georgia 30912.
Wei-Hua WuFrom the Department of Neuroscience and Regenerative Medicine and Department of Neurology, Medical College of Georgia, Georgia Regents University, Augusta, Georgia 30912.
Bo-Shiun ChenFrom the Department of Neuroscience and Regenerative Medicine and Department of Neurology, Medical College of Georgia, Georgia Regents University, Augusta, Georgia 30912. Electronic address: bochen@gru.edu.
Augusta University · US

Funding

Trafficking and Regulation of the NMDA Receptor Subunit NR2CR00NS057266 · NINDS · AUGUSTA UNIVERSITY · PI CHEN, BO-SHIUN · 2010 to 2012
$743k
The function of a single-component chromatin remodeling protein Fun30 in vivoK22CA122453 · NCI · AUGUSTA UNIVERSITY · PI WU, WEI-HUA E · 2010 to 2012
$451k
NCI NIH HHS 1K22CA122453NCI NIH HHS K22 CA122453NINDS NIH HHS R00 NS057266NINDS NIH HHS R00NS057266
6 · The paper itself

Abstract

Synapse-associated protein 102 (SAP102) is a scaffolding protein abundantly expressed early in development that mediates glutamate receptor trafficking during synaptogenesis. Mutations in human SAP102 have been reported to cause intellectual disability, which is consistent with its important role during early postnatal development. SAP102 contains PDZ, SH3, and guanylate kinase (GK)-like domains, which mediate specific protein-protein interactions. SAP102 binds directly to N-methyl-D-aspartate receptors (NMDARs), anchors receptors at synapses, and facilitates transduction of NMDAR signals. Proper localization of SAP102 at the postsynaptic density is essential to these functions. However, how SAP102 is targeted to synapses is unclear. In the current study we find that synaptic localization of SAP102 is regulated by alternative splicing. The SAP102 splice variant that possesses a C-terminal insert (I2) between the SH3 and GK domains is highly enriched at dendritic spines. We also show that there is an intramolecular interaction between the SH3 and GK domains in SAP102 but that the I2 splicing does not influence SH3-GK interaction. Previously, we have shown that SAP102 expression promotes spine lengthening. We now find that the spine lengthening effect is independent of the C-terminal alternative splicing of SAP102. In addition, expression of I2-containing SAP102 isoforms is regulated developmentally. Knockdown of endogenous I2-containing SAP102 isoforms differentially affect NMDAR surface expression in a subunit-specific manner. These data shed new light on the role of SAP102 in the regulation of NMDAR trafficking.

Indexed as

Alternative SplicingAnimalsHEK293 CellsHumansNeuropeptidesNuclear ProteinsPost-Synaptic DensityProtein TransportRatsRats, Sprague-DawleyReceptors, N-Methyl-D-Aspartatesrc Homology DomainsTranscription FactorsDLG3 protein, humanDlg3 protein, ratNeuropeptidesNuclear ProteinsReceptors, N-Methyl-D-AspartateTranscription FactorsGlutamate ReceptorMAGUKNMDAPDZ DomainProtein SplicingProtein TargetingSAP102Scaffold Protein

Identifiers

PMID25555912
PMCPMC4335245
OpenAlexW2084627991

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.