Presynaptic PTP sigma regulates postsynaptic NMDA receptor function through direct adhesion-independent mechanisms
- Authors
- Kim, Kyungdeok; Shin, Wangyong; Kang, Muwon; Lee, Suho; Kim, Doyoun; Kang, Ryeonghwa; Jung, Yewon; Cho, Yisul; Yang, Esther; Kim, Hyun; Bae, Yong Chul; Kim, Eunjoon
- Issue Date
- 6-3월-2020
- Publisher
- ELIFE SCIENCES PUBLICATIONS LTD
- Citation
- ELIFE, v.9
- Indexed
- SCIE
SCOPUS
- Journal Title
- ELIFE
- Volume
- 9
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/57315
- DOI
- 10.7554/eLife.54224
- ISSN
- 2050-084X
- 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 PTP sigma, 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 PTP sigma, suggesting that the cytoplasmic domains of PTP sigma, 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 PTP sigma-mutant mice. Behaviorally, PTP sigma-dependent NMDAR regulation is important for social and reward-related novelty recognition. These results suggest that presynaptic PTP sigma regulates postsynaptic NMDAR function through trans-synaptic and direct adhesion-independent mechanisms and novelty recognition in social and reward contexts.
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Collections - Graduate School > Department of Biomedical Sciences > 1. Journal Articles
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