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2015 ; 12
(10
): 1618-30
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Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory
Synapse Development and Locomotion
#MMPMID26321637
Li Y
; Zhang P
; Choi TY
; Park SK
; Park H
; Lee EJ
; Lee D
; Roh JD
; Mah W
; Kim R
; Kim Y
; Kwon H
; Bae YC
; Choi SY
; Craig AM
; Kim E
Cell Rep
2015[Sep]; 12
(10
): 1618-30
PMID26321637
show ga
Synaptic adhesion molecules regulate diverse aspects of synapse development and
plasticity. SALM3 is a PSD-95-interacting synaptic adhesion molecule known to
induce presynaptic differentiation in contacting axons, but little is known about
its presynaptic receptors and in vivo functions. Here, we identify an interaction
between SALM3 and LAR family receptor protein tyrosine phosphatases (LAR-RPTPs)
that requires the mini-exon B splice insert in LAR-RPTPs. In addition,
SALM3-dependent presynaptic differentiation requires all three types of
LAR-RPTPs. SALM3 mutant (Salm3(-/-)) mice display markedly reduced excitatory
synapse number but normal synaptic plasticity in the hippocampal CA1 region.
Salm3(-/-) mice exhibit hypoactivity in both novel and familiar environments but
perform normally in learning and memory tests administered. These results suggest
that SALM3 regulates excitatory synapse development and locomotion behavior.