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AMPA Receptor Surface Expression Is Regulated by S-Nitrosylation of Thorase and Transnitrosylation of NSF

Title
AMPA Receptor Surface Expression Is Regulated by S-Nitrosylation of Thorase and Transnitrosylation of NSF
Authors
Umanah, George K. E.Ghasemi, MehdiYin, XilingChang, MelissaKim, Jin WanZhang, JianminMa, EricaScarffe, Leslie A.Lee, Yun-IlChen, RongTangella, KavyaMcNamara, AmyAbalde-Atristain, LeireDar, Mohamad A.Bennett, SamuelCortes, MarisolAndrabi, Shaida A.Doulias, Paschalis-ThomasIschiropoulos, HarryDawson, Ted M.Dawson, Valina L.
DGIST Authors
Lee, Yun-Il
Issue Date
2020-11
Citation
Cell Reports, 33(5), 108329
Type
Article
Article Type
Article
Author Keywords
major depressive disorderanheodnianucleus accumbensTac1Substance PNK1 receptor
Keywords
ETHYLMALEIMIDE-SENSITIVE FACTORSYNAPTIC PLASTICITYGLUR2 SUBUNITPROTEINATPASEDOMAINPHOSPHORYLATIONMODULATIONMECHANISMSCOMPLEX
ISSN
2211-1247
Abstract
Umanah et al. show that the S-nitrosylation of Thorase and the transnitrosylation of NSF are responsible for NMDAR-activated trafficking of AMPARs underlying synaptic plasticity. © 2020 The Author(s) The regulation of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) trafficking affects multiple brain functions, such as learning and memory. We have previously shown that Thorase plays an important role in the internalization of AMPARs from the synaptic membrane. Here, we show that N-methyl-D-aspartate receptor (NMDAR) activation leads to increased S-nitrosylation of Thorase and N-ethylmaleimide-sensitive factor (NSF). S-nitrosylation of Thorase stabilizes Thorase-AMPAR complexes and enhances the internalization of AMPAR and interaction with protein-interacting C kinase 1 (PICK1). S-nitrosylated NSF is dependent on the S-nitrosylation of Thorase via trans-nitrosylation, which modulates the surface insertion of AMPARs. In the presence of the S-nitrosylation-deficient C137L Thorase mutant, AMPAR trafficking, long-term potentiation, and long-term depression are impaired. Overall, our data suggest that both S-nitrosylation and interactions of Thorase and NSF/PICK1 are required to modulate AMPAR-mediated synaptic plasticity. This study provides critical information that elucidates the mechanism underlying Thorase and NSF-mediated trafficking of AMPAR complexes. © 2020 The Author(s)
URI
http://hdl.handle.net/20.500.11750/12774
DOI
10.1016/j.celrep.2020.108329
Publisher
Cell Press
Related Researcher
Files:
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Collection:
Division of Biotechnology1. Journal Articles


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