Elongation Factor 2 and Fragile X Mental Retardation Protein Control the Dynamic Translation of Arc/Arg3.1 Essential for mGluR-LTD
Open accessAbstract
Group I metabotropic glutamate receptors (mGluR) induce long-term depression (LTD) that requires protein synthesis. Here, we demonstrate that Arc/Arg3.1 is translationally induced within 5 min of mGluR activation, and this response is essential for mGluR-dependent LTD. The increase in Arc/Arg3.1 translation requires eEF2K, a Ca(2+)/calmodulin-dependent kinase that binds mGluR and dissociates upon mGluR activation, whereupon it phosphorylates eEF2. Phospho-eEF2 acts to slow the elongation step of translation and inhibits general protein synthesis but simultaneously increases Arc/Arg3.1 translation. Genetic deletion of eEF2K results in a selective deficit of rapid mGluR-dependent Arc/Arg3.1 translation and mGluR-LTD. This rapid translational mechanism is disrupted in the fragile X disease mouse (Fmr1 KO) in which mGluR-LTD does not require de novo protein synthesis but does require Arc/Arg3.1. We propose a model in which eEF2K-eEF2 and FMRP coordinately control the dynamic translation of Arc/Arg3.1 mRNA in dendrites that is critical for synapse-specific LTD.
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Translation of Arc mRNA is enhanced during and crucial for mGluR-dependent LTD.
“Translation of Arc mRNA is enhanced during, and crucial for, mGluR-dependent LTD59,60.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [59]
In Fmr1 knockout mice, dynamic translation of Arc mRNA in response to stimulation is impaired, and basal Arc protein level in dendrites is elevated.
“In Fmr1 knockout mice, the dynamic translation of Arc mRNA in response to stimulation is impaired59,61, and the basal level of the Arc protein in dendrites is elevated61.”
From Activity-dependent neuronal signalling and autism spectrum disorder (2013) · cites this paper as [59]
Under physiological conditions, NMDAR-dependent activation of eEF2K results in inactivation (phosphorylation) of eEF2, leading to the blockade of the elongation phase of protein synthesis and thus inhibition of protein translation.
“Under physiological conditions, NMDAR-dependent activation of eEF2K results in inactivation (phosphorylation) of eEF2 leading to the blockade of the elongation phase of protein synthesis and thus inhibition of protein translation 166, 167.”
From Mechanisms of ketamine action as an antidepressant (2018) · cites this paper as [167]
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Self-citation
- Authors
- Park, S., Park, J. M., Kim, S., Kim, J.-A., Shepherd, J. D., Smith-Hicks, C. L., Chowdhury, S., Kaufmann, W., Kuhl, D., Ryazanov, A. G., Huganir, R. L., Linden, D. J., & Worley, P. F.
- Affiliations
- Johns Hopkins University (US)
- Massachusetts Institute of Technology (US)
- Freie Universität Berlin (DE)
- University of Medicine and Dentistry of New Jersey (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Worley, Paul F.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 59
- Issue
- 1
- Pages
- 70-83
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC2743934
- OpenAlex
- W2100699923
- Cited by
- 516
- References
- 59
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 15 · 2023: 18 · 2022: 18 · 2021: 35 · 2020: 35 · 2019: 29 · 2018: 30 · 2017: 36 · 2016: 31 · 2015: 32 · 2014: 30 · 2013: 30 · 2012: 43
- FWCI
- 17.01
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1842 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health (MH053608, MH068830, MH51106)
- National Institute on Aging (AG019890, GM057300)
- FRAXA Research Foundation
- National Institute of Development Administration (DA00266)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- Arc/Arg3.1, eEF2K, elongation factor 2, FMRP, group I metabotropic glutamate receptors, long-term depression, translational regulation, dendritic protein synthesis, Fmr1 knockout mice, calcium/calmodulin-dependent protein kinase
- MeSH terms
- Animals, Animals, Newborn, Cells, Cultured, Cycloheximide, Cytoskeletal Proteins, Dose-Response Relationship, Radiation, Electric Stimulation, Gene Expression Regulation, Hippocampus, Male, Models, Biological, Nerve Tissue Proteins, Neurons, Protein Synthesis Inhibitors, Protein Biosynthesis, Long-Term Potentiation, Receptors, AMPA, Mice, Knockout, Patch-Clamp Techniques, Excitatory Amino Acid Agents, Excitatory Postsynaptic Potentials, Peptide Elongation Factor 2, Protein Transport, Mice, Fragile X Messenger Ribonucleoprotein 1, In Vitro Techniques
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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