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LAR-RPTP Clustering Is Modulated by Competitive Binding between Synaptic Adhesion Partners and Heparan Sulfate

Title
LAR-RPTP Clustering Is Modulated by Competitive Binding between Synaptic Adhesion Partners and Heparan Sulfate
Authors
Won, Seoung YounKim, Cha YeonKim, DoyounKo, JaewonUm, Ji WonLee, Sung BaeBuck, MatthiasKim, EunjoonHeo, Won DoLee, Jie-OhKim, Ho Min
DGIST Authors
Ko, JaewonUm, Ji WonLee, Sung Bae
Issue Date
2017-10
Citation
Frontiers in Molecular Neuroscience, 10
Type
Article
Article Type
Article
Keywords
ArchitectureComplexCrystal StructureDependent Transsynaptic AdhesionHeparan SulfateHigher-Order ClusteringLAR-RPTPsMidline Axon GuidanceMoleculePostsynaptic LigandProtein-Tyrosine-PhosphatasesProteoglycansPtp-SigmaReceptorStructural BasisSynaptic Adhesion Molecules
ISSN
1662-5099
Abstract
The leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are cellular receptors of heparan sulfate (HS) and chondroitin sulfate (CS) proteoglycans that direct axonal growth and neuronal regeneration. LAR-RPTPs are also synaptic adhesion molecules that form trans-synaptic adhesion complexes by binding to various postsynaptic adhesion ligands, such as Slit- and Trk-like family of proteins (Slitrks), IL-1 receptor accessory protein-like 1 (IL1RAPL1), interleukin-1 receptor accessory protein (IL-1RAcP) and neurotrophin receptor tyrosine kinase C (TrkC), to regulate synaptogenesis. Here, we determined the crystal structure of the human LAR-RPTP/IL1RAPL1 complex and found that lateral interactions between neighboring LAR-RPTP/IL1RAPL1 complexes in crystal lattices are critical for the higher-order assembly and synaptogenic activity of these complexes. Moreover, we found that LAR-RPTP binding to the postsynaptic adhesion ligands, Slitrk3, IL1RAPL1 and IL-1RAcP, but not TrkC, induces reciprocal higher-order clustering of trans-synaptic adhesion complexes. Although LAR-RPTP clustering was induced by either HS or postsynaptic adhesion ligands, the dominant binding of HS to the LAR-RPTP was capable of dismantling pre-established LAR-RPTP-mediated trans-synaptic adhesion complexes. These findings collectively suggest that LAR-RPTP clustering for synaptogenesis is modulated by a complex synapse-organizing protein network. © 2017 Won, Kim, Kim, Ko, Um, Lee, Buck, Kim, Heo, Lee and Kim.
URI
http://hdl.handle.net/20.500.11750/4730
DOI
10.3389/fnmol.2017.00327
Publisher
Frontiers Media S.A.
Related Researcher
  • Author Lee, Sung Bae SB LAB(Lab of Neurodegenerative diseases and Aging)
  • Research Interests Cellular mechanism of neurodegenerative diseases; Neuronal maintenance and remodeling; 퇴행성 뇌질환의 세포기전; 신경계 유지 및 리모델링 연구
Files:
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Collection:
Brain and Cognitive SciencesUm Laboratory1. Journal Articles
Brain and Cognitive SciencesSB LAB(Lab of Neurodegenerative diseases and Aging)1. Journal Articles


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