Presynaptic PTPσ regulates postsynaptic NMDA receptor function through direct adhesion-independent mechanisms
| العنوان: | Presynaptic PTPσ regulates postsynaptic NMDA receptor function through direct adhesion-independent mechanisms |
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| المؤلفون: | Wangyong Shin, Suho Lee, Esther Yang, Doyoun Kim, Ryeonghwa Kang, Hyun Kim, Yisul Cho, Muwon Kang, Eunjoon Kim, Yewon Jung, Kyungdeok Kim, Yong Chul Bae |
| المصدر: | eLife, Vol 9 (2020) eLife |
| بيانات النشر: | eLife Sciences Publications Ltd, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, tyrosine phosphatase, Mouse, QH301-705.5, Science, Mice, Transgenic, Neuroimaging, Protein tyrosine phosphatase, Receptors, N-Methyl-D-Aspartate, Synaptic Transmission, novelty recognition, General Biochemistry, Genetics and Molecular Biology, Synapse, 03 medical and health sciences, Mice, 0302 clinical medicine, Postsynaptic potential, Neurotransmitter receptor, Animals, Biology (General), long-term potentiation, synaptic plasticity, General Immunology and Microbiology, Cell adhesion molecule, Chemistry, General Neuroscience, Receptor-Like Protein Tyrosine Phosphatases, Class 2, synaptic adhesion, Long-term potentiation, General Medicine, nmda receptors, 030104 developmental biology, Gene Expression Regulation, nervous system, Synaptic plasticity, Synapses, NMDA receptor, Medicine, Neuroscience, Open Field Test, 030217 neurology & neurosurgery, Research Article |
| الوصف: | 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. |
| اللغة: | English |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d92c9275d747277f0645761d97faa35d https://elifesciences.org/articles/54224 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....d92c9275d747277f0645761d97faa35d |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |