The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 118; no. 9; pp. 1 - 10
• Main Authors: Chao-Hua, Jiang, Wei, Mengping, Zhang, Chen, Shi, Yun Stone
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 02.03.2021
• Subjects: Animals; Biological Sciences; Embryo, Mammalian; Excitatory Postsynaptic Potentials - genetics; Female; Gene Expression Regulation; Genes, Reporter; Green Fluorescent Proteins - genetics; Green Fluorescent Proteins - metabolism; HEK293 Cells; Hippocampus - cytology; Hippocampus - metabolism; Humans; Long-Term Potentiation - genetics; Luminescent Proteins - genetics; Luminescent Proteins - metabolism; Male; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Mice; Primary Cell Culture; Protein Domains; Pyramidal Cells - cytology; Pyramidal Cells - metabolism; Receptors, AMPA - genetics; Receptors, AMPA - metabolism; Red Fluorescent Protein; Single-Cell Analysis; Synapses; LTP; AMPA receptors; GluA1; neuroplastin; amino-terminal domain

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 rema...