Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion

Yan Li; Peng Zhang; Tae Yong Choi; Sook Kyung Park; Hanwool Park; Eun Jae Lee; Dongsoo Lee; Junyeop Daniel Roh; Won Mah; Ryunhee Kim; Yangsik Kim; Harah Kwon; Yong Chul Bae; Se Young Choi; Ann Marie Craig; Eunjoon Kim

doi:10.1016/j.celrep.2015.08.002

Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion

Yan Li, Peng Zhang, Tae Yong Choi, Sook Kyung Park, Hanwool Park, Eun Jae Lee, Dongsoo Lee, Junyeop Daniel Roh, Won Mah, Ryunhee Kim, Yangsik Kim, Harah Kwon, Yong Chul Bae, Se Young Choi, Ann Marie Craig, Eunjoon Kim

Department of Dentistry

Research output: Contribution to journal › Article › peer-review

59 Scopus citations

Abstract

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. SALM3 is a postsynaptic adhesion molecule known to regulate synapse development, but the underlying mechanism remains unclear. Li et al. find that SALM3 interacts with presynaptic LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) in a splicing-dependent manner. In addition, they show that SALM3-mutant mice display reduced excitatory synapse number and hypoactivity.

Original language	English
Pages (from-to)	1618-1630
Number of pages	13
Journal	Cell Reports
Volume	12
Issue number	10
DOIs	https://doi.org/10.1016/j.celrep.2015.08.002
State	Published - 8 Sep 2015

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Li, Y., Zhang, P., Choi, T. Y., Park, S. K., Park, H., Lee, E. J., Lee, D., Roh, J. D., Mah, W., Kim, R., Kim, Y., Kwon, H., Bae, Y. C., Choi, S. Y., Craig, A. M., & Kim, E. (2015). Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion. Cell Reports, 12(10), 1618-1630. https://doi.org/10.1016/j.celrep.2015.08.002

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title = "Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion",

abstract = "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. SALM3 is a postsynaptic adhesion molecule known to regulate synapse development, but the underlying mechanism remains unclear. Li et al. find that SALM3 interacts with presynaptic LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) in a splicing-dependent manner. In addition, they show that SALM3-mutant mice display reduced excitatory synapse number and hypoactivity.",

author = "Yan Li and Peng Zhang and Choi, {Tae Yong} and Park, {Sook Kyung} and Hanwool Park and Lee, {Eun Jae} and Dongsoo Lee and Roh, {Junyeop Daniel} and Won Mah and Ryunhee Kim and Yangsik Kim and Harah Kwon and Bae, {Yong Chul} and Choi, {Se Young} and Craig, {Ann Marie} and Eunjoon Kim",

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AU - Li, Yan

AU - Zhang, Peng

AU - Choi, Tae Yong

AU - Park, Sook Kyung

AU - Park, Hanwool

AU - Lee, Eun Jae

AU - Lee, Dongsoo

AU - Roh, Junyeop Daniel

AU - Mah, Won

AU - Kim, Ryunhee

AU - Kim, Yangsik

AU - Kwon, Harah

AU - Bae, Yong Chul

AU - Choi, Se Young

AU - Craig, Ann Marie

AU - Kim, Eunjoon

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N2 - 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. SALM3 is a postsynaptic adhesion molecule known to regulate synapse development, but the underlying mechanism remains unclear. Li et al. find that SALM3 interacts with presynaptic LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) in a splicing-dependent manner. In addition, they show that SALM3-mutant mice display reduced excitatory synapse number and hypoactivity.

AB - 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. SALM3 is a postsynaptic adhesion molecule known to regulate synapse development, but the underlying mechanism remains unclear. Li et al. find that SALM3 interacts with presynaptic LAR family receptor protein tyrosine phosphatases (LAR-RPTPs) in a splicing-dependent manner. In addition, they show that SALM3-mutant mice display reduced excitatory synapse number and hypoactivity.

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Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion

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