한빛사 논문
Abstract
Eunkyung Lie1, Ji Seung Ko2, Su-Yeon Choi3, Junyeop Daniel Roh3, Yi Sul Cho4, Ran Noh5, Doyoun Kim3, Yan Li3, Hyeyeon Kang6, Tae-Yong Choi7, Jungyong Nam1, Won Mah4, Dongmin Lee8, Seong-Gyu Lee9, Ho Min Kim9, Hyun Kim8, Se-Young Choi7, Ji Won Um6, Myoung-Goo Kang5,9, Yong Chul Bae4, Jaewon Ko2 & Eunjoon Kim1,3,*
1 Department of Biological Sciences, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea. 2 Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea. 3 Center for Synaptic Brain Dysfunctions, Institute for Basic Science, Daejeon 305-701, Korea. 4 Department of Anatomy and Neurobiology, School of Dentistry, Kyungpook National University, Daegu 700-412, Korea. 5 Center for Cognition and Sociality, Institute for Basic Science, Daejeon 305-701, Korea. 6 Department of Physiology and BK21 PLUS Project to Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea. 7 Department of Physiology, Seoul National University School of Dentistry, Seoul 110-749, Korea. 8 Department of Anatomy and Division of Brain Korea 21, Biomedical Science, College of Medicine, Korea University, Seoul 136-705, Korea. 9 Graduate School of Medical Science and Engineering, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea.
*Correspondence to : Eunjoon Kim
Abstract
Synaptic adhesion molecules regulate various aspects of synapse development, function and plasticity. These functions mainly involve trans-synaptic interactions and positive regulations, whereas cis-interactions and negative regulation are less understood. Here we report that SALM4, a member of the SALM/Lrfn family of synaptic adhesion molecules, suppresses excitatory synapse development through cis inhibition of SALM3, another SALM family protein with synaptogenic activity. Salm4-mutant (Salm4-/-) mice show increased excitatory synapse numbers in the hippocampus. SALM4 cis-interacts with SALM3, inhibits trans-synaptic SALM3 interaction with presynaptic LAR family receptor tyrosine phosphatases and suppresses SALM3-dependent presynaptic differentiation. Importantly, deletion of Salm3 in Salm4-/- mice (Salm3-/-; Salm4-/-) normalizes the increased excitatory synapse number. These results suggest that SALM4 negatively regulates excitatory synapses via cis inhibition of the trans-synaptic SALM3-LAR adhesion.
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