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

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

doi:10.1038/ncomms12328

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

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 BaeJaewon Ko, Eunjoon Kim

Department of Dentistry

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

26 Scopus citations

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.

Original language	English
Article number	12328
Journal	Nature Communications
Volume	7
DOIs	https://doi.org/10.1038/ncomms12328
State	Published - 2 Aug 2016

Access to Document

10.1038/ncomms12328

Cite this

Lie, E., Ko, J. S., Choi, S. Y., Roh, J. D., Cho, Y. S., Noh, R., Kim, D., Li, Y., Kang, H., Choi, T. Y., Nam, J., Mah, W., Lee, D., Lee, S. G., Kim, H. M., Kim, H., Choi, S. Y., Um, J. W., Kang, M. G., ... Kim, E. (2016). SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion. Nature Communications, 7, Article 12328. https://doi.org/10.1038/ncomms12328

@article{71b117dfbf5f474d80a61bee057d82a8,

title = "SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion",

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.",

author = "Eunkyung Lie and Ko, {Ji Seung} and Choi, {Su Yeon} and Roh, {Junyeop Daniel} and Cho, {Yi Sul} and Ran Noh and Doyoun Kim and Yan Li and Hyeyeon Kang and Choi, {Tae Yong} and Jungyong Nam and Won Mah and Dongmin Lee and Lee, {Seong Gyu} and Kim, {Ho Min} and Hyun Kim and Choi, {Se Young} and Um, {Ji Won} and Kang, {Myoung Goo} and Bae, {Yong Chul} and Jaewon Ko and Eunjoon Kim",

note = "Publisher Copyright: {\textcopyright} The Author(s) 2016.",

year = "2016",

month = aug,

day = "2",

doi = "10.1038/ncomms12328",

language = "English",

volume = "7",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Publishing Group",

}

Lie, E, Ko, JS, Choi, SY, Roh, JD, Cho, YS, Noh, R, Kim, D, Li, Y, Kang, H, Choi, TY, Nam, J, Mah, W, Lee, D, Lee, SG, Kim, HM, Kim, H, Choi, SY, Um, JW, Kang, MG, Bae, YC, Ko, J & Kim, E 2016, 'SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion', Nature Communications, vol. 7, 12328. https://doi.org/10.1038/ncomms12328

TY - JOUR

T1 - SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion

AU - Lie, Eunkyung

AU - Ko, Ji Seung

AU - Choi, Su Yeon

AU - Roh, Junyeop Daniel

AU - Cho, Yi Sul

AU - Noh, Ran

AU - Kim, Doyoun

AU - Li, Yan

AU - Kang, Hyeyeon

AU - Choi, Tae Yong

AU - Nam, Jungyong

AU - Mah, Won

AU - Lee, Dongmin

AU - Lee, Seong Gyu

AU - Kim, Ho Min

AU - Kim, Hyun

AU - Choi, Se Young

AU - Um, Ji Won

AU - Kang, Myoung Goo

AU - Bae, Yong Chul

AU - Ko, Jaewon

AU - Kim, Eunjoon

PY - 2016/8/2

Y1 - 2016/8/2

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84982672436&partnerID=8YFLogxK

U2 - 10.1038/ncomms12328

DO - 10.1038/ncomms12328

M3 - Article

C2 - 27480238

AN - SCOPUS:84982672436

SN - 2041-1723

VL - 7

JO - Nature Communications

JF - Nature Communications

M1 - 12328

ER -

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this