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Presynaptic PTPs regulates postsynaptic NMDA receptor function through direct adhesion-independent mechanisms

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Title
Presynaptic PTPs regulates postsynaptic NMDA receptor function through direct adhesion-independent mechanisms
Author(s)
Kyungdeok Kim; Wangyong Shin; Muwon Kang; Suho Lee; Doyoun Kim; Ryeonghwa Kang; Yewon Jung; Yisul Cho; Esther Yang; Hyun Kim; Yong Chul Bae; Eunjoon Kim
Publication Date
2020-03
Journal
ELIFE, v.9, no., pp.e54224 -
Publisher
ELIFE SCIENCES PUBLICATIONS LTD
Abstract
Synaptic adhesion molecules regulate synapse development and function. However, whether and how presynaptic adhesion molecules regulate postsynaptic NMDAR function remains largely unclear. Presynaptic LAR family receptor tyrosine phosphatases (LAR-RPTPs) regulate synapse development through mechanisms that include trans-synaptic adhesion; however, whether they regulate postsynaptic receptor functions remains unknown. Here we report that presynaptic PTPσ, a LAR-RPTP, enhances postsynaptic NMDA receptor (NMDAR) currents and NMDAR-dependent synaptic plasticity in the hippocampus. This regulation does not involve trans-synaptic adhesions of PTPσ, suggesting that the cytoplasmic domains of PTPσ, known to have tyrosine phosphatase activity and mediate protein-protein interactions, are important. In line with this, phosphotyrosine levels of presynaptic proteins, including neurexin-1, are strongly increased in PTPσ-mutant mice. Behaviorally, PTPσ-dependent NMDAR regulation is important for social and reward-related novelty recognition. These results suggest that presynaptic PTPσ regulates postsynaptic NMDAR function through trans-synaptic and direct adhesion-independent mechanisms and novelty recognition in social and reward contexts.Copyright Kim et al.
URI
https://pr.ibs.re.kr/handle/8788114/7141
ISSN
2050-084X
Appears in Collections:
Center for Synaptic Brain Dysfunctions(시냅스 뇌질환 연구단) > Journal Papers (저널논문)
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