Regulation of AMPA Receptor Trafficking by Protein Ubiquitination
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The molecular mechanisms underlying plastic changes in the strength and connectivity of excitatory synapses have been studied extensively for the past few decades and remain the most attractive cellular models of learning and memory. One of the major mechanisms that regulate synaptic plasticity is the dynamic adjustment of the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptor content on the neuronal plasma membrane. The expression of surface AMPA receptors (AMPARs) is controlled by the delicate balance between the biosynthesis, dendritic transport, exocytosis, endocytosis, recycling and degradation of the receptors. These processes are dynamically regulated by AMPAR interacting proteins as well as by various post-translational modifications that occur on their cytoplasmic domains. In the last few years, protein ubiquitination has emerged as a major regulator of AMPAR intracellular trafficking. Dysregulation of AMPAR ubiquitination has also been implicated in the pathophysiology of Alzheimer's disease. Here we review recent advances in the field and provide insights into the role of protein ubiquitination in regulating AMPAR membrane trafficking and function. We also discuss how aberrant ubiquitination of AMPARs contributes to the pathogenesis of various neurological disorders, including Alzheimer's disease, chronic stress and epilepsy.
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All four AMPAR subunits are ubiquitinated, with major sites on GluA1 and GluA2 mapped to GluA1 K868 and GluA2 K870/K882.
“All four AMPAR subunit are also ubiquitinated. The major sites of ubiquitination on GluA1 and GluA2 have been mapped to GluA1 K868 and GluA2 K870/K882 (Widagdo et al., 2015, Widagdo et al., 2017, Lussier et al., 2015).”
From The AMPA Receptor Code of Synaptic Plasticity (2018) · cites this paper as Widagdo et al., 2017
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- Authors
- Widagdo, J., Guntupalli, S., Jang, S. E., & Anggono, V.
- Affiliations
- The University of Queensland (AU)
- Corresponding author
- Anggono, Victor
- Venue
- Frontiers in Molecular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2017-10-26
- Volume
- 10
- Pages
- 347-347
- ISSN
- 1662-5099 (ISSN-L)
- PMC
- PMC5662755
- OpenAlex
- W2766178360
- Cited by
- 68
- References
- 82
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 8 · 2023: 10 · 2022: 6 · 2021: 9 · 2020: 8 · 2019: 8 · 2018: 7
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Molecular Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Health and Medical Research Council (GNT1083209, GNT1099114)
- John T. Reid Charitable Trusts
- Australian Research Council (DP170102402, DE170100112)
- Alzheimer’s Australia Dementia Research Foundation (DGP14-57)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- AMPA receptors, ubiquitination, receptor trafficking, synaptic plasticity, excitatory synapses, post-translational modification, receptor internalization, receptor recycling, Alzheimer's disease, chronic stress, epilepsy, neurological disorders
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