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SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development.

 Yeonsoo Choi  ;  Jungyong Nam  ;  Daniel J. Whitcomb  ;  Yoo Sung Song  ;  Doyoun Kim  ;  Sangmin Jeon  ;  Ji Won Um  ;  Seong-Gyu Lee  ;  Jooyeon Woo  ;  Seok-Kyu Kwon  ;  Yan Li  ;  Won Mah  ;  Ho Min Kim  ;  Jaewon Ko  ;  Kwangwook Cho  ;  Eunjoon Kim 
 SCIENTIFIC REPORTS, Vol.6 : 26676, 2016 
Journal Title
Issue Date
Alternative Splicing/physiology* ; Animals ; Axons/metabolism* ; Cell Adhesion Molecules, Neuronal/genetics ; Cell Adhesion Molecules, Neuronal/metabolism* ; Mice ; Receptor-Like Protein Tyrosine Phosphatases, Class 2/genetics ; Receptor-Like Protein Tyrosine Phosphatases, Class 2/metabolism* ; Synapses/genetics ; Synapses/metabolism* ; Synaptic Transmission/physiology*
Synaptogenic adhesion molecules play critical roles in synapse formation. SALM5/Lrfn5, a SALM/Lrfn family adhesion molecule implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons, but its presynaptic ligand remains unknown. We found that SALM5 interacts with the Ig domains of LAR family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPδ, and PTPσ). These interactions are strongly inhibited by the splice insert B in the Ig domain region of LAR-RPTPs, and mediate SALM5-dependent presynaptic differentiation in contacting axons. In addition, SALM5 regulates AMPA receptor-mediated synaptic transmission through mechanisms involving the interaction of postsynaptic SALM5 with presynaptic LAR-RPTPs. These results suggest that postsynaptic SALM5 promotes synapse development by trans-synaptically interacting with presynaptic LAR-RPTPs and is important for the regulation of excitatory synaptic strength.
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1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers
Yonsei Authors
Um, Ji Won(엄지원)
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