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

Yeonsoo Choi; Jungyong Nam; Daniel Whitcomb; Yoo Sung Song; Doyoun Kim; Sangmin Jeon; Ji Won Um; Sang-Gyu Lee; Jooyeon Woo; Seok-Kyu Kwon; Yan Li; Won  Ma; Ho Min Kim; Jaewon Ko; Kwangwook Cho; Eunjoon Kim

doi:10.1038/srep26676

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

Yeonsoo Choi, Jungyong Nam, Daniel Whitcomb, Yoo Sung Song, Doyoun Kim, Sangmin Jeon, Ji Won Um, Sang-Gyu Lee, Jooyeon Woo, Seok-Kyu Kwon, Yan Li, Won Ma, Ho Min Kim, Jaewon Ko, Kwangwook Cho, Eunjoon Kim

Research output: Contribution to journal › Article (Academic Journal) › peer-review

36 Citations (Scopus)

315 Downloads (Pure)

Abstract

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.

Original language	English
Article number	26676
Journal	Scientific Reports
Volume	6
DOIs	https://doi.org/10.1038/srep26676
Publication status	Published - 26 May 2016

Access to Document

10.1038/srep26676

srep26676
This is the final published version of the article (version of record). It first appeared online via Nature at http://www.nature.com/srep/2016/160526/srep26676/full/srep26676. Please refer to any applicable terms of use of the publisher.
Final published version, 2.01 MBLicence: CC BY

Fingerprint Dive into the research topics of 'SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development'. Together they form a unique fingerprint.

1 Finished

How does stress regulate tau-associated synaptic function?
Whitcomb, D.
1/01/16 → 31/12/18
Project: Research

Dr Daniel Whitcomb
- D.J.Whitcomb@bristol.ac.uk
- Bristol Medical School (THS) - Senior Lecturer in Translational Neuroscience
- Laboratories for Integrative Neuroscience and Endocrinology
- Translational Neuroscience Research Group
Person: Academic , Member

Cite this

Choi, Yeonsoo ; Nam, Jungyong ; Whitcomb, Daniel ; Sung Song, Yoo ; Kim, Doyoun ; Jeon, Sangmin ; Um, Ji Won ; Lee, Sang-Gyu ; Woo, Jooyeon ; Kwon, Seok-Kyu ; Li, Yan ; Ma, Won ; Kim, Ho Min ; Ko, Jaewon ; Cho, Kwangwook ; Kim, Eunjoon. / SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development. In: Scientific Reports. 2016 ; Vol. 6.

@article{311e58611f3f4552b2f20c037a785abb,

title = "SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development",

abstract = "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.",

author = "Yeonsoo Choi and Jungyong Nam and Daniel Whitcomb and {Sung Song}, Yoo and Doyoun Kim and Sangmin Jeon and Um, {Ji Won} and Sang-Gyu Lee and Jooyeon Woo and Seok-Kyu Kwon and Yan Li and Won Ma and Kim, {Ho Min} and Jaewon Ko and Kwangwook Cho and Eunjoon Kim",

year = "2016",

month = may,

day = "26",

doi = "10.1038/srep26676",

language = "English",

volume = "6",

journal = "Scientific Reports",

issn = "2045-2322",

publisher = "Springer Nature",

}

SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development. / Choi, Yeonsoo; Nam, Jungyong; Whitcomb, Daniel; Sung Song, Yoo; Kim, Doyoun; Jeon, Sangmin; Um, Ji Won; Lee, Sang-Gyu; Woo, Jooyeon; Kwon, Seok-Kyu; Li, Yan; Ma, Won ; Kim, Ho Min; Ko, Jaewon; Cho, Kwangwook; Kim, Eunjoon.

In: Scientific Reports, Vol. 6, 26676, 26.05.2016.

Research output: Contribution to journal › Article (Academic Journal) › peer-review

TY - JOUR

T1 - SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development

AU - Choi, Yeonsoo

AU - Nam, Jungyong

AU - Whitcomb, Daniel

AU - Sung Song, Yoo

AU - Kim, Doyoun

AU - Jeon, Sangmin

AU - Um, Ji Won

AU - Lee, Sang-Gyu

AU - Woo, Jooyeon

AU - Kwon, Seok-Kyu

AU - Li, Yan

AU - Ma, Won

AU - Kim, Ho Min

AU - Ko, Jaewon

AU - Cho, Kwangwook

AU - Kim, Eunjoon

PY - 2016/5/26

Y1 - 2016/5/26

N2 - 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.

AB - 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.

U2 - 10.1038/srep26676

DO - 10.1038/srep26676

M3 - Article (Academic Journal)

C2 - 27225731

VL - 6

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 26676

ER -

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

Abstract

Access to Document

How does stress regulate tau-associated synaptic function?

Dr Daniel Whitcomb

Cite this