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Mol Cells. 2018 Jul 31;41(7):622-630. doi: 10.14348/molcells.2018.0202. Epub 2018 Jul 11.

Structural Basis for LAR-RPTP-Mediated Synaptogenesis.

Author information

1
Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
2
Graduate School of Medical Science & Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
3
Center for Synaptic Brain Dysfunctions, Institute for Basic Science (IBS), Daejeon 34141, Korea.

Abstract

Leukocyte common antigen-related protein tyrosine phosphatases (LAR-RPTPs) are cellular receptors of heparan sulfate (HS) and chondroitin sulfate (CS) proteoglycans that regulate neurite outgrowth and neuronal regeneration. LAR-RPTPs have also received particular attention as the major presynaptic hubs for synapse organization through selective binding to numerous postsynaptic adhesion partners. Recent structural studies on LAR-RPTP-mediated trans-synaptic adhesion complexes have provided significant insight into the molecular basis of their specific interactions, the key codes for their selective binding, as well as the higher-order clustering of LAR-RPTPs necessary for synaptogenic activity. In this review, we summarize the structures of LAR-RPTPs in complex with various postsynaptic adhesion partners and discuss the molecular mechanisms underlying LAR-RPTP-mediated synaptogenesis.

KEYWORDS:

LAR-RPTPs; LAR-RPTP–mediated trans-synaptic adhesion complex; heparan sulfate; higher-order clustering; synaptic adhesion molecules

PMID:
30008201
PMCID:
PMC6078854
DOI:
10.14348/molcells.2018.0202
[Indexed for MEDLINE]
Free PMC Article

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