气候变化领域集成服务门户(CCPortal): The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65

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DOI	10.1073/pnas.2019194118
	The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65
	Jiang C.-H.; Wei M.; Zhang C.; Shi Y.S.
发表日期	2021
ISSN	00278424
卷号	118 期号:9
英文摘要	Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Amino-terminal domain; AMPA receptors; GluA1; LTP; Neuroplastin
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180446
作者单位	State Key Laboratory of Pharmaceutical Biotechnology, Department of Neurology, Affiliated Drum Tower Hospital of Nanjing University Medical School, Nanjing University, Nanjing, 210032, China; Ministry of Education Key Laboratory of Model Animal for Disease Study, Model Animal Research Center, Nanjing University, Nanjing, 210032, China; School of Basic Medical Sciences, Beijing Key Laboratory of Neural Regeneration and Repair, Advanced Innovation Center for Human Brain Protection, Capital Medical University, Beijing, 100069, China; Institute for Brain Sciences, Nanjing University, Nanjing, 210032, China; Chemistry and Biomedicine Innovation Center, Nanjing University, Nanjing, 210032, China
推荐引用方式 GB/T 7714	Jiang C.-H.,Wei M.,Zhang C.,et al. The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65[J],2021,118(9).
APA	Jiang C.-H.,Wei M.,Zhang C.,&Shi Y.S..(2021).The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65.Proceedings of the National Academy of Sciences of the United States of America,118(9).
MLA	Jiang C.-H.,et al."The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65".Proceedings of the National Academy of Sciences of the United States of America 118.9(2021).