Neurexin-neuroligin adhesions capture surface-diffusing AMPA receptors through PSD-95 scaffolds (Q28505247)

3

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Florian Levet

6

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Christel Poujol

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author name string

Magali Mondin

1

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24 January 2017

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Virginie Labrousse

2

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Martin Heine

4

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Béatrice Tessier

5

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Christophe Blanchet

8

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Olivier Thoumine

10

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Daniel Choquet

9

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language of work or name

English

0 references

publication date

21 September 2011

1 reference

24 January 2017

Journal of Neuroscience

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volume

31

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issue

38

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page(s)

13500-13515

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describes a project that uses

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ImageJ

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inferred from PubMed Central ID database lookup

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Lateral diffusion drives constitutive exchange of AMPA receptors at dendritic spines and is regulated by spine morphology.

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Alternative N-terminal domains of PSD-95 and SAP97 govern activity-dependent regulation of synaptic AMPA receptor function

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Local sharing as a predominant determinant of synaptic matrix molecular dynamics

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Neuroligins determine synapse maturation and function

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Synapse-specific and developmentally regulated targeting of AMPA receptors by a family of MAGUK scaffolding proteins.

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Rapid redistribution of synaptic PSD-95 in the neocortex in vivo

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NMDA receptor surface mobility depends on NR2A-2B subunits

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Neurexin-neuroligin signaling in synapse development

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The interaction between Stargazin and PSD-95 regulates AMPA receptor surface trafficking

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Diffusional trapping of GluR1 AMPA receptors by input-specific synaptic activity

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Extracellular interactions between GluR2 and N-cadherin in spine regulation

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Surface mobility of postsynaptic AMPARs tunes synaptic transmission

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PSD-95 promotes synaptogenesis and multiinnervated spine formation through nitric oxide signaling.

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Destabilization of the postsynaptic density by PSD-95 serine 73 phosphorylation inhibits spine growth and synaptic plasticity

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Activity-independent and subunit-specific recruitment of functional AMPA receptors at neurexin/neuroligin contacts

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Differential trafficking of AMPA and NMDA receptors by SAP102 and PSD-95 underlies synapse development

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An unbiased expression screen for synaptogenic proteins identifies the LRRTM protein family as synaptic organizers

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Subunit composition of synaptic AMPA receptors revealed by a single-cell genetic approach

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Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenesis

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Brain extracellular matrix affects AMPA receptor lateral mobility and short-term synaptic plasticity.

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The stoichiometry of AMPA receptors and TARPs varies by neuronal cell type.

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Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation

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Neuroligin 2 drives postsynaptic assembly at perisomatic inhibitory synapses through gephyrin and collybistin

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Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn

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LRRTM2 interacts with Neurexin1 and regulates excitatory synapse formation

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LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development

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CaMKII triggers the diffusional trapping of surface AMPARs through phosphorylation of stargazin

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Neurexin-neuroligin cell adhesion complexes contribute to synaptotropic dendritogenesis via growth stabilization mechanisms in vivo

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Imaging activity-dependent regulation of neurexin-neuroligin interactions using trans-synaptic enzymatic biotinylation

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Functional dependence of neuroligin on a new non-PDZ intracellular domain

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Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons.

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Binding of neuroligins to PSD-95

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10.1523/JNEUROSCI.6439-10.2011

Identifiers

DOI

2 references

24 January 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6623291&resulttype=core&format=json

15 May 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=PMCID:PMC6623291&resulttype=core&format=json

15 May 2020

2 references

24 January 2017