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Nat. Neurosci., Published online 23 November 2015 | doi:10.1038/nn.4176
Synaptic adhesion molecule IgSF11 regulates synaptic transmission and plasticity
Abstract
Seil Jang1,16, Daeyoung Oh2,3,16, Yeunkum Lee4,16, Eric Hosy5,6,16, Hyewon Shin2, Christoph van Riesen7, Daniel Whitcomb8,9, Julia M Warburton8, Jihoon Jo8,10, Doyoun Kim4, Sun Gyun Kim4, Seung Min Um1, Seok-kyu Kwon1, Myoung-Hwan Kim11,12, Junyeop Daniel Roh4, Jooyeon Woo1, Heejung Jun13, Dongmin Lee14, Won Mah15, Hyun Kim14, Bong-Kiun Kaang13, Kwangwook Cho8,9, Jeong-Seop Rhee7,*, Daniel Choquet5,6,* & Eunjoon Kim1,4,*
1Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea. 2Department of Biomedical Sciences, KAIST, Daejeon, Korea. 3Department of Psychiatry, CHA Bundang Medical Center, CHA University, Seoul, Korea. 4Center for Synaptic Brain Dysfunctions, Institute for Basic Science (IBS), Daejeon, Korea. 5University of Bordeaux, Interdisciplinary Institute for Neuroscience, Bordeaux, France. 6CNRS UMR 5297, Bordeaux, France. 7Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Gottingen, Germany. 8School of Clinical Sciences, Faculty of Medicine and Dentistry, University of Bristol, Bristol, UK. 9Centre for Synaptic Plasticity, University of Bristol, Bristol, UK. 10Department of Biomedical Sciences, Chonnam National University Medical School, Gwangju, South Korea. 11Department of Physiology, Seoul National University College of Medicine, Seoul, Republic of Korea. 12Seoul National University Bundang Hospital, Seongnam, Gyeonggi, Republic of Korea. 13Biological Sciences, College of Natural Sciences, Seoul National University, Seoul, Korea. 14Department of Anatomy and Division of Brain Korea 21 Biomedical Science, College of Medicine, Korea University, Seoul, Korea. 15Department of Anatomy and Neurobiology, School of Dentistry, Kyungpook National University, Daegu, Korea. 16These authors contributed equally to this work.
*Correspondence to : Eunjoon Kim or Daniel Choquet or Jeong-Seop Rhee
Abstract
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.
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.
논문정보
- Research article
- 2015년 11월 (BRIC 등록일 2015-11-26)
- 국내(교신)+국외 연구진
- 생명과학 > 생리학
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