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

Authors: Choi, Yeonsoo  Nam, Jungyong  Whitcomb, Daniel J  Song, Yoo Sung  Kim, Doyoun  Jeon, Sangmin  Um, Ji Won  Lee, Seong-Gyu  Woo, Jooyeon  Kwon, Seok-Kyu  Li, Yan  Mah, Won  Kim, Ho Min  Ko, Jaewon  Cho, Kwangwook  Kim, Eunjoon 
Citation: Choi Y, etal., Sci Rep. 2016 May 26;6:26676. doi: 10.1038/srep26676.
Pubmed: (View Article at PubMed) PMID:27225731
DOI: Full-text: DOI:10.1038/srep26676

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, PTPd, and PTPs). 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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RGD Object Information
RGD ID: 13702436
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.