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PTPσ functions as a presynaptic receptor for the glypican-4/LRRTM4 complex and is essential for excitatory synaptic transmission

Authors
 Ji Seung Ko  ;  Gopal Pramanik  ;  Ji Won Um  ;  Ji Seon Shim  ;  Dongmin Lee  ;  Kee Hun Kim  ;  Gug-Young Chung  ;  Giuseppe Condomitti  ;  Ho Min Kim  ;  Hyun Kim  ;  Joris de Wit  ;  Kang-Sik Park  ;  Katsuhiko Tabuchi  ;  Jaewon Ko 
Citation
 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol.112(6) : 1874-1879, 2015 
Journal Title
 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 
ISSN
 0027-8424 
Issue Date
2015
MeSH
Analysis of Variance ; Animals ; Blotting, Western ; Brain/metabolism* ; Chromatography, Affinity ; Chromatography, High Pressure Liquid ; Gene Knockdown Techniques ; Genetic Vectors/genetics ; Glypicans/metabolism* ; Heparitin Sulfate/metabolism ; Immunohistochemistry ; Immunoprecipitation ; In Situ Hybridization ; Mass Spectrometry ; Multiprotein Complexes/metabolism* ; Oligonucleotides/genetics ; Presynaptic Terminals/physiology ; Proteins/metabolism* ; Rats ; Receptor-Like Protein Tyrosine Phosphatases, Class 2/genetics ; Receptor-Like Protein Tyrosine Phosphatases, Class 2/metabolism* ; Synaptic Transmission/physiology*
Keywords
LRRTM4 ; PTPσ ; glypican ; heparan sulfate ; synaptic cell adhesion
Abstract
Leukocyte common antigen-related receptor protein tyrosine phosphatases--comprising LAR, PTPδ, and PTPσ--are synaptic adhesion molecules that organize synapse development. Here, we identify glypican 4 (GPC-4) as a ligand for PTPσ. GPC-4 showed strong (nanomolar) affinity and heparan sulfate (HS)-dependent interaction with the Ig domains of PTPσ. PTPσ bound only to proteolytically cleaved GPC-4 and formed additional complex with leucine-rich repeat transmembrane protein 4 (LRRTM4) in rat brains. Moreover, single knockdown (KD) of PTPσ, but not LAR, in cultured neurons significantly reduced the synaptogenic activity of LRRTM4, a postsynaptic ligand of GPC-4, in heterologous synapse-formation assays. Finally, PTPσ KD dramatically decreased both the frequency and amplitude of excitatory synaptic transmission. This effect was reversed by wild-type PTPσ, but not by a HS-binding-defective PTPσ mutant. Our results collectively suggest that presynaptic PTPσ, together with GPC-4, acts in a HS-dependent manner to maintain excitatory synapse development and function.
Files in This Item:
T201500344.pdf Download
DOI
10.1073/pnas.1410138112
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers
Yonsei Authors
Um, Ji Won(엄지원)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/139415
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