한빛사논문
- 조회2,962
Abstract
Jooyeon Woo1,2, Seok-Kyu Kwon1,2, Jungyong Nam1,2, Seungwon Choi1,2, Hideto Takahashi3, Dilja Krueger4, Joohyun Park5, Yeunkum Lee1,2, Jin Young Bae6, Dongmin Lee7,8, Jaewon Ko9, Hyun Kim7,8, Myoung-Hwan Kim5, Yong Chul Bae6, Sunghoe Chang5, Ann Marie Craig3, and Eunjoon Kim1,2
1Center for Synaptic Brain Dysfunctions, Institute for Basic Science (IBS), Daejeon 305-701, South Korea
2Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, South Korea
3Brain Research Centre and Department of Psychiatry, University of British Columbia, Vancouver, British Columbia, Canada
4Max Planck Institute of Experimental Medicine, Department of Molecular Neurobiology, D-37075 Gottingen, Germany 5Department of Physiology and Biomedical Sciences, Seoul National University College of Medicine, Seoul 110-799, South Korea
6Department of Anatomy and Neurobiology, School of Dentistry, Kyungpook National University, Daegu 700-412, South Korea
7Department of Anatomy and 8Division of Brain Korea 21 Project for Biomedical Science, College of Medicine, Korea University, Seoul 136-705, South Korea
9Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, South Korea
J. Woo, S.-K. Kwon, J. Nam, S. Choi, and H. Takahashi contributed equally to this paper.
Correspondence to Eunjoon or Ann Marie Craig:
Abstract
Synaptic adhesion molecules regulate diverse aspects of synapse formation and maintenance. Many known synaptic adhesion molecules localize at excitatory synapses, whereas relatively little is known about inhibitory synaptic adhesion molecules. Here we report that IgSF9b is a novel, brain-specific, homophilic adhesion molecule that is strongly expressed in GABAergic interneurons. IgSF9b was preferentially localized at inhibitory synapses in cultured rat hippocampal and cortical interneurons and was required for the development of inhibitory synapses onto interneurons. IgSF9b formed a subsynaptic domain distinct from the GABAA receptor- and gephyrin-containing domain, as indicated by super-resolution imaging. IgSF9b was linked to neuroligin 2, an inhibitory synaptic adhesion molecule coupled to gephyrin, via the multi-PDZ protein S-SCAM. IgSF9b and neuroligin 2 could reciprocally cluster each other. These results suggest a novel mode of inhibitory synaptic organization in which two subsynaptic domains, one containing IgSF9b for synaptic adhesion and the other containing gephyrin and GABAA receptors for synaptic transmission, are interconnected through S-SCAM and neuroligin 2.
논문정보
- Research article
- 2013년 06월 (BRIC 등록일 2013-06-14)
- 국내(교신)+국외 연구진
- 생명과학 > 생리학
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