Evidence map›Paper›PMID 31291981›Full record

ArticleMolecular brain2019

NMDAR mediated translation at the synapse is regulated by MOV10 and FMRP.

Preeti Madhav Kute, Sarayu Ramakrishna, Nagammal Neelagandan, Sumantra Chattarji, Ravi S Muddashetty

Open access · goldAbstract read
In one paragraph

Article in Molecular brain, 2019. 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
2.7field-weighted citation impact, top 10% 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, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. NMDAR mediated dynamic changes in mScientific reports · 2022
    Article
  9. Review
  10. Unwinding the roles of RNA helicase MOV10.Wiley interdisciplinary reviews. RNA · 2022
    Review
  11. APOE4 Affects Basal and NMDAR-Mediated Protein Synthesis in Neurons by Perturbing Calcium Homeostasis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  12. Article
  13. Article
  14. The Role of Dynamic miRISC During Neuronal Development.Frontiers in molecular biosciences · 2020
    Review
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

5 authors at 3 institutions in 2 countries.

Preeti Madhav KuteCentre for Brain Development and Repair (CBDR), Institute for Stem Cell Science and Regenerative Medicine (inStem), Bangalore, 560065, India.
Sarayu RamakrishnaCentre for Brain Development and Repair (CBDR), Institute for Stem Cell Science and Regenerative Medicine (inStem), Bangalore, 560065, India.
Nagammal NeelagandanCentre for Brain Development and Repair (CBDR), Institute for Stem Cell Science and Regenerative Medicine (inStem), Bangalore, 560065, India.
Sumantra ChattarjiCentre for Brain Development and Repair (CBDR), Institute for Stem Cell Science and Regenerative Medicine (inStem), Bangalore, 560065, India.
Ravi S MuddashettyCentre for Brain Development and Repair (CBDR), Institute for Stem Cell Science and Regenerative Medicine (inStem), Bangalore, 560065, India. ravism@instem.res.in.ORCID 0000-0002-1373-6194
Institute for Stem Cell Biology and Regenerative Medicine · INNational Centre for Biological Sciences · INUniversity of Trans-Disciplinary Health Sciences and Technology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein synthesis is crucial for maintaining synaptic plasticity and synaptic signalling. Here we have attempted to understand the role of RNA binding proteins, Fragile X Mental Retardation Protein (FMRP) and Moloney Leukemia Virus 10 (MOV10) protein in N-Methyl-D-Aspartate Receptor (NMDAR) mediated translation regulation. We show that FMRP is required for translation downstream of NMDAR stimulation and MOV10 is the key specificity factor in this process. In rat cortical synaptoneurosomes, MOV10 in association with FMRP and Argonaute 2 (AGO2) forms the inhibitory complex on a subset of NMDAR responsive mRNAs. On NMDAR stimulation, MOV10 dissociates from AGO2 and promotes the translation of its target mRNAs. FMRP is required to form MOV10-AGO2 inhibitory complex and to promote translation of MOV10 associated mRNAs. Phosphorylation of FMRP appears to be the potential switch for NMDAR mediated translation and in the absence of FMRP, the distinct translation response to NMDAR stimulation is lost. Thus, FMRP and MOV10 have an important regulatory role in NMDAR mediated translation at the synapse.

Indexed as

Protein BiosynthesisAnimalsArgonaute ProteinsDisks Large Homolog 4 ProteinDNA HelicasesFragile X Messenger Ribonucleoprotein 1PhosphorylationPolyribosomesProtein BindingRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateRNA, MessengerSynapsesUp-RegulationAgo2 protein, ratArgonaute ProteinsDisks Large Homolog 4 ProteinDlg4 protein, ratDNA HelicasesFragile X Messenger Ribonucleoprotein 1MOV10 protein, ratReceptors, N-Methyl-D-AspartateRNA, MessengerFMRP/MOV10/NMDAR mediated translation

Identifiers

PMID31291981
PMCPMC6617594
OpenAlexW2958860944

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.