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Synaptic adhesion molecule IgSF11 regulates synaptic transmission and plasticity.

Authors: Jang, S  Oh, D  Lee, Y  Hosy, E  Shin, H  Van Riesen, C  Whitcomb, D  Warburton, JM  Jo, J  Kim, D  Kim, SG  Um, SM  Kwon, SK  Kim, MH  Roh, JD  Woo, J  Jun, H  Lee, D  Mah, W  Kim, H  Kaang, BK  Cho, K  Rhee, JS  Choquet, D  Kim, E 
Citation: Jang S, etal., Nat Neurosci. 2016 Jan;19(1):84-93. doi: 10.1038/nn.4176. Epub 2015 Nov 23.
Pubmed: (View Article at PubMed) PMID:26595655
DOI: Full-text: DOI:10.1038/nn.4176

Synaptic adhesion molecules regulate synapse development and plasticity through mechanisms that include trans-synaptic adhesion and recruitment of diverse synaptic proteins. We found that the immunoglobulin superfamily member 11 (IgSF11), a homophilic adhesion molecule that preferentially expressed in the brain, is a dual-binding partner of the postsynaptic scaffolding protein PSD-95 and AMPA glutamate receptors (AMPARs). IgSF11 required PSD-95 binding for its excitatory synaptic localization. In addition, IgSF11 stabilized synaptic AMPARs, as determined by IgSF11 knockdown-induced suppression of AMPAR-mediated synaptic transmission and increased surface mobility of AMPARs, measured by high-throughput, single-molecule tracking. IgSF11 deletion in mice led to the suppression of AMPAR-mediated synaptic transmission in the dentate gyrus and long-term potentiation in the CA1 region of the hippocampus. IgSF11 did not regulate the functional characteristics of AMPARs, including desensitization, deactivation or recovery. These results suggest that IgSF11 regulates excitatory synaptic transmission and plasticity through its tripartite interactions with PSD-95 and AMPARs.


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CRRD Object Information
CRRD ID: 11085699
Created: 2016-06-01
Species: All species
Last Modified: 2016-06-01
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.