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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 Youn; Kim, Cha Yeon; Kim, Doyoun; Ko, Jaewon; Um, Ji Won; Lee, Sung Bae; Buck, Matthias; Kim, Eunjoon; Heo, Won Do; Lee, Jie-Oh; Kim, Ho Min
- DGIST Authors
- Won, Seoung Youn; Kim, Cha Yeon; Kim, Doyoun; Ko, Jaewon; Um, Ji Won; Lee, Sung Bae; Buck, Matthias; Kim, Eunjoon; Heo, Won Do; Lee, Jie-Oh; Kim, Ho Min
- Issue Date
- 2017-10
- Citation
- Frontiers in Molecular Neuroscience, 10
- Type
- Article
- Article Type
- Article
- Author Keywords
- LAR-RPTPs; postsynaptic ligand; synaptic adhesion molecules; higher-order clustering; heparan sulfate; crystal structure
- Keywords
- DEPENDENT TRANSSYNAPTIC ADHESION; PROTEIN-TYROSINE-PHOSPHATASES; MIDLINE AXON GUIDANCE; PTP-SIGMA; STRUCTURAL BASIS; RECEPTOR; COMPLEX; PROTEOGLYCANS; ARCHITECTURE; MOLECULE
- 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
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Lee, Sung Bae
Laboratory of Neurodegenerative Diseases and Aging
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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:
- Department of Brain SciencesLaboratory of Synapse Formation and Function1. Journal Articles
Department of Brain SciencesSynapse Disorder Laboratory1. Journal Articles
Department of Brain SciencesLaboratory of Neurodegenerative Diseases and Aging1. Journal Articles
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