Evidence map›Paper›PMID 28508887›Full record

ArticleNature communications2017

An evolutionary switch in ND2 enables Src kinase regulation of NMDA receptors.

David P Scanlon, Alaji Bah, Mickaël Krzeminski, Wenbo Zhang, Heather L Leduc-Pessah, Yi Na Dong, Julie D Forman-Kay, Michael W Salter

Open access · goldAbstract readValidation Study
In one paragraph

Article in Nature communications, 2017. 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
0.4field-weighted citation impact, top 47% 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, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Metabotropic NMDAR Signaling Contributes to Sex Differences in Synaptic Plasticity and Episodic Memory.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  6. Src dependency of the regulation of LTP by alternative splicing ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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

8 authors at 3 institutions in 1 country.

David P ScanlonProgram in Neurosciences &Mental Health, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Alaji BahProgram in Molecular Medicine, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Mickaël KrzeminskiProgram in Molecular Medicine, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Wenbo ZhangProgram in Neurosciences &Mental Health, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Heather L Leduc-PessahProgram in Neurosciences &Mental Health, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Yi Na DongProgram in Neurosciences &Mental Health, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Julie D Forman-KayProgram in Molecular Medicine, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Michael W SalterProgram in Neurosciences &Mental Health, The Hospital for Sick Children, 686 Bay St, Toronto, Ontario, Canada M5G 0A4.
Hospital for Sick Children · CAUniversity of Toronto · CACanada Research Chairs · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The non-receptor tyrosine kinase Src is a key signalling hub for upregulating the function of N-methyl D-aspartate receptors (NMDARs). Src is anchored within the NMDAR complex via NADH dehydrogenase subunit 2 (ND2), a mitochondrially encoded adaptor protein. The interacting regions between Src and ND2 have been broadly identified, but the interaction between ND2 and the NMDAR has remained elusive. Here we generate a homology model of ND2 and dock it onto the NMDAR via the transmembrane domain of GluN1. This interaction is enabled by the evolutionary loss of three helices in bilaterian ND2 proteins compared to their ancestral homologues. We experimentally validate our model and demonstrate that blocking this interaction with an ND2 fragment identified in our experimental studies prevents Src-mediated upregulation of NMDAR currents in neurons. Our findings establish the mode of interaction between an NMDAR accessory protein with one of the core subunits of the receptor.

Indexed as

Evolution, MolecularModels, MolecularAnimalsElectron Transport Complex IFemaleHEK293 CellsHippocampusHumansNADH DehydrogenaseNeuronsPhosphorylationPrimary Cell CultureProtein DomainsRatsRats, WistarReceptors, N-Methyl-D-AspartateElectron Transport Complex INADH DehydrogenaseReceptors, N-Methyl-D-Aspartatesrc-Family Kinases

Identifiers

PMID28508887
PMCPMC5440837
OpenAlexW2615563660

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.