The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65.
TLDR
In this paper, the amino-terminal domain (ATD) of GluA1 is found to be essential for long-term potentiation (LTP) maintenance.Abstract:
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.read more
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AMPA receptor trafficking and LTP: Carboxy-termini, amino-termini and TARPs
TL;DR: In this paper, an updated AMPAR trafficking and LTP model was proposed, which incorporates both extracellular as well as intracellular mechanisms, based on recent research reviewed in this special issue on AMPA receptors.
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Biology of AMPA receptor interacting proteins - From biogenesis to synaptic plasticity.
TL;DR: An overview of the catalogue of AMPAR interacting proteins and how they contribute to the complex biology of this central glutamate receptor can be found in this article, where an array of transmembrane proteins operate as auxiliary subunits that in addition to receptor trafficking and stabilization also substantially impact AMPAR gating and pharmacology.
Journal ArticleDOI
X-linked neonatal-onset epileptic encephalopathy associated with a gain-of-function variant p.R660T in GRIA3.
Jia Hui Sun,Jiang Chen,Fernando Eduardo Ayala Valenzuela,Carolyn Brown,Diane Masser-Frye,Marilyn C. Jones,Leslie Patrón Romero,Berardo Rinaldi,Wenhui Laura Li,Qing Qing Li,Dan Wu,Bénédicte Gérard,Erin Thorpe,Allan Bayat,Yun Stone Shi +14 more
TL;DR: In this article, a de novo pathogenic missense variant in GRIA3 (c.1979G>C; p. R660T) was identified in a 1-year-old female patient with severe epilepsy and global developmental delay.
Journal ArticleDOI
AMPA receptor anchoring at CA1 synapses is determined by N-terminal domain and TARP γ8 interactions.
TL;DR: In this article, the authors compare the contributions of three AMPAR interaction domains controlling transmission at hippocampal CA1 synapses, and show that the AMPAR C-termini play only a modulatory role, whereas the extracellular N-terminal domain (NTD) and PDZ interactions of the auxiliary subunit TARP γ8 are both crucial, and each is sufficient to maintain transmission.
Journal ArticleDOI
Ca2+ signaling in postsynaptic neurons: Neuroplastin-65 regulates the interplay between plasma membrane Ca2+ ATPases and ionotropic glutamate receptors.
Ayse Malci,Xiao Lin,Rodrigo Sandoval,Eckart D. Gundelfinger,Michael Naumann,Constanze I. Seidenbecher,Rodrigo Herrera-Molina +6 more
TL;DR: In this paper , the authors showed that Np65-specific extracellular domain of Np55-PMCA complexes can be used to regulate the duration and amplitude of cytosolic Ca2+ transients in dendrites and spines of hippocampal neurons.
References
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