Evidence map›Paper›PMID 34251337›Full record

ArticleeLife2021

Sorting nexin-27 regulates AMPA receptor trafficking through the synaptic adhesion protein LRFN2.

Kirsty J McMillan, Paul J Banks, Francesca Ln Hellel, Ruth E Carmichael, Thomas Clairfeuille, Ashley J Evans, Kate J Heesom, Philip Lewis, Brett M Collins, Zafar I Bashir and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  7. TauCell death & disease · 2024
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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

13 authors at 2 institutions in 2 countries.

Kirsty J McMillan *School of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-4619-3309
Paul J Banks *School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, United Kingdom.
Francesca Ln HellelSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.
Ruth E CarmichaelSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0003-2665-2966
Thomas ClairfeuilleInstitute for Molecular Bioscience, The University of Queensland, Queensland, Australia.
Ashley J EvansSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-6658-2176
Kate J HeesomProteomics facility, School of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-5418-5392
Philip LewisProteomics facility, School of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-2868-2459
Brett M CollinsInstitute for Molecular Bioscience, The University of Queensland, Queensland, Australia.ORCID 0000-0002-6070-3774
Zafar I BashirSchool of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, United Kingdom.
Jeremy M HenleySchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0003-3589-8335
Kevin A WilkinsonSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-8115-8592
Peter J CullenSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-9070-8349
University of Bristol · GBThe University of Queensland · AU

Funding

Biotechnology and Biological Sciences Research Council BB/R00787X/1Medical Research Council MR/L003791/1Medical Research Council MR/L007363/1Medical Research Council MR/P018807/1Wellcome TrustWellcome Trust 104568/Z/14/2Wellcome Trust 220260/Z/20/Z
6 · The paper itself

Abstract

The endosome-associated cargo adaptor sorting nexin-27 (SNX27) is linked to various neuropathologies through sorting of integral proteins to the synaptic surface, most notably AMPA receptors. To provide a broader view of SNX27-associated pathologies, we performed proteomics in rat primary neurons to identify SNX27-dependent cargoes, and identified proteins linked to excitotoxicity, epilepsy, intellectual disabilities, and working memory deficits. Focusing on the synaptic adhesion molecule LRFN2, we established that SNX27 binds to LRFN2 and regulates its endosomal sorting. Furthermore, LRFN2 associates with AMPA receptors and knockdown of LRFN2 results in decreased surface AMPA receptor expression, reduced synaptic activity, and attenuated hippocampal long-term potentiation. Overall, our study provides an additional mechanism by which SNX27 can control AMPA receptor-mediated synaptic transmission and plasticity indirectly through the sorting of LRFN2 and offers molecular insight into the perturbed function of SNX27 and LRFN2 in a range of neurological conditions.

Indexed as

AnimalsEndosomesHippocampusHumansLong-Term PotentiationMembrane GlycoproteinsMemory DisordersNerve Tissue ProteinsNeuronsProtein TransportProteomicsRatsReceptors, AMPASorting NexinsSynaptic TransmissionLRFN2 protein, humanMembrane GlycoproteinsNerve Tissue ProteinsReceptors, AMPASNX27 protein, humanSnx27 protein, ratSorting NexinsAMPA receptorscell biologyhumanLRFN2membrane traffickingneuroscienceratSNX27

Identifiers

PMID34251337
PMCPMC8296521
OpenAlexW3182146502

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.