Synaptic adhesion molecule IgSF11 regulates synaptic transmission and plasticity

Seil Jang, Daeyoung Oh, Yeunkum Lee, Eric Hosy, Hyewon Shin, Christoph Van Riesen, Daniel Whitcomb, Julia M. Warburton, Jihoon Jo, Doyoun Kim, Sun Gyun Kim, Seung Min Um, Seok Kyu Kwon, Myoung Hwan Kim, Junyeop Daniel Roh, Jooyeon Woo, Heejung Jun, Dongmin Lee, Won Mah, Hyun KimBong Kiun Kaang, Kwangwook Cho, Jeong Seop Rhee, Daniel Choquet, Eunjoon Kim

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)84-93
Number of pages10
JournalNature Neuroscience
Issue number1
Publication statusPublished - 2015 Dec 29

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© 2016 Nature America, Inc.

ASJC Scopus subject areas

  • General Neuroscience


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