ArticleeLife2023
Regulation of different phases of AMPA receptor intracellular transport by 4.1N and SAP97.
Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- GluA1 C80 Peptide Impairs Short-Term Spatial Memory in Mice by Interfering with the 4.1N Binding Site.Neuroscience bulletin · 2026Article
- The GluA1 cytoplasmic tail regulates intracellular AMPA receptor trafficking and synaptic transmission onto dentate gyrus GABAergic interneurons, gating response to novelty.Molecular psychiatry · 2026Article
- Sex differences in AMPA receptor trafficking proteins.Biology of sex differences · 2026Review
- AMPA Receptors in Synaptic Plasticity, Memory Function, and Brain Diseases.Cellular and molecular neurobiology · 2025Review
- Article
- Activity-dependent diffusion trapping of AMPA receptors as a key step for expression of early LTP.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Calcium-permeable AMPA and kainate receptors of GABAergic neurons.Biophysical reviews · 2024Review
- Protein 4.1N Plays a Cell Type-Specific Role in Hippocampal Glutamatergic Synapse Regulation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Regulation of different phases of AMPA receptor intracellular transport by 4.1N and SAP97.eLife · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Changes in the number of synaptic AMPA receptors underlie many forms of synaptic plasticity. These variations are controlled by an interplay between their intracellular transport (IT), export to the plasma membrane (PM), stabilization at synapses, and recycling. The cytosolic C-terminal domain of the AMPAR GluA1 subunit is specifically associated with 4.1 N and SAP97. We analyze how interactions between GluA1 and 4.1N or SAP97 regulate IT and exocytosis in basal conditions and after cLTP induction. The down-regulation of 4.1N or SAP97 decreases GluA1 IT properties and export to the PM. The total deletion of its C-terminal fully suppresses its IT. Our results demonstrate that during basal transmission, the binding of 4.1N to GluA1 allows their exocytosis whereas the interaction with SAP97 is essential for GluA1 IT. During cLTP, the interaction of 4.1N with GluA1 allows its IT and exocytosis. Our results identify the differential roles of 4.1N and SAP97 in the control of various phases of GluA1 IT.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.