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SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion

Authors
 Eunkyung Lie  ;  Ji Seung Ko  ;  Su-Yeon Choi  ;  Junyeop Daniel Roh  ;  Yi Sul Cho  ;  Ran Noh  ;  Doyoun Kim  ;  Yan Li  ;  Hyeyeon Kang  ;  Tae-Yong Choi  ;  Jungyong Nam  ;  Won Mah  ;  Dongmin Lee  ;  Seong-Gyu Lee  ;  Ho Min Kim  ;  Hyun Kim  ;  Se-Young Choi  ;  Ji Won Um  ;  Myoung-Goo Kang  ;  Yong Chul Bae  ;  Jaewon Ko  ;  Eunjoon Kim 
Citation
 NATURE COMMUNICATIONS, Vol.7 : 12328-12342, 2016 
Journal Title
 NATURE COMMUNICATIONS 
Issue Date
2016
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.
Files in This Item:
T201602723.pdf Download
DOI
10.1038/ncomms12328
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers
Yonsei Authors
Um, Ji Won(엄지원)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/151710
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