Synaptic adhesion molecule IgSF11 regulates synaptic transmission and plasticity

Autor: Junyeop Daniel Roh, Myoung Hwan Kim, Hyewon Shin, Christoph Van Riesen, Yeunkum Lee, Daniel J. Whitcomb, Seok-Kyu Kwon, Jeong-Seop Rhee, Julia M. Warburton, Seil Jang, Daeyoung Oh, Doyoun Kim, Jihoon Jo, Heejung Jun, Sun-Gyun Kim, Eunjoon Kim, Won Mah, Hyun Kim, Bong-Kiun Kaang, Jooyeon Woo, Dongmin Lee, Kwangwook Cho, Daniel Choquet, Eric Hosy, Seung Min Um
Rok vydání: 2015
Předmět:
Zdroj: Nature Neuroscience. 19:84-93
ISSN: 1546-1726
1097-6256
Popis: Synaptic adhesion molecules regulate synapse development and plasticity through mechanisms including trans-synaptic adhesion and recruitment of diverse synaptic proteins. We report here that the immunoglobulin superfamily member 11 (IgSF11), a homophilic adhesion molecule preferentially expressed in the brain, is a novel and dual-binding partner of the postsynaptic scaffolding protein PSD-95 and AMPAR glutamate receptors (AMPARs). IgSF11 requires PSD-95 binding for its excitatory synaptic localization. In addition, IgSF11 stabilizes synaptic AMPARs, as shown 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 leads to suppression of AMPAR-mediated synaptic transmission in the dentate gyrus and long-term potentiation in the CA1 region of the hippocampus. IgSF11 does 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.
Databáze: OpenAIRE