Ezrin mediates tethering of the γ-aminobutyric acid transporter GAT1 to actin filaments via a C-terminal PDZ-interacting domain
Open accessAbstract
A high density of neurotransmitter transporters on axons and presynaptic boutons is required for the efficient clearance of neurotransmitters from the synapse. Therefore, regulators of transporter trafficking (insertion, retrieval, and confinement) can play an important role in maintaining the transporter density necessary for effective function. We determined the interactions that confine GAT1 at the membrane by investigating the lateral mobility of GAT1-yellow fluorescent protein-8 (YFP8) expressed in neuroblastoma 2a cells. Through fluorescence recovery after photobleaching, we found that a significant fraction ( approximately 50%) of membrane-localized GAT1 is immobile on the time scale investigated ( approximately 150 s). The mobility of the transporter can be increased by depolymerizing actin or by interrupting the GAT1 postsynaptic density 95/Discs large/zona occludens 1 (PDZ)-interacting domain. Microtubule depolymerization, in contrast, does not affect GAT1 membrane mobility. We also identified ezrin as a major GAT1 adaptor to actin. Förster resonance energy transfer suggests that GAT1-YFP8 and cyan fluorescent (CFP) tagged ezrin (ezrin-CFP) exist within a complex that has a Förster resonance energy transfer efficiency of 19% +/- 2%. This interaction can be diminished by disrupting the actin cytoskeleton. In addition, the disruption of actin results in a >3-fold increase in gamma-aminobutyric acid uptake, apparently via a mechanism distinct from the PDZ-interacting protein. Our data reveal that actin confines GAT1 to the plasma membrane via ezrin, and this interaction is mediated through the PDZ-interacting domain of GAT1.
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Under the transient transfection conditions used in Neuro-2a cells, membrane protein expression levels have not reached maximum, rendering the optical assays sensitive to mutations or pharmacological agents.
“Previous studies using both fluorescent gamma amino butyric acid transporters and fluorescent nAChRs established that, under the conditions used, membrane protein expression levels have not reached maximum (Drenan et al., 2008; Imoukhuede et al., 2009; Moss et al., 2009; Son et al., 2009).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Imoukhuede et al., 2009
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- Authors
- Imoukhuede, P. I., Moss, F. J., Michael, D. J., Chow, R. H., & Lester, H. A.
- Affiliations
- California Institute of Technology (US)
- University of Southern California (US)
- Corresponding author
- Lester, Henry A.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2009-04
- Volume
- 96
- Issue
- 7
- Pages
- 2949-2960
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC2711277
- OpenAlex
- W2132505087
- Cited by
- 29
- References
- 64
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 2 · 2017: 2 · 2015: 2 · 2014: 3
- FWCI
- 0.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- California Institute of Technology
- National Institutes of Health (DA-09121, DK-60623, NS-11756)
- American Heart Association
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- ezrin, GABA transporter 1, actin cytoskeleton, membrane tethering, postsynaptic density, neurotransmitter uptake, actin depolymerization
- MeSH terms
- Ezrin, Actins, Animals, Biological Transport, Cytoskeletal Proteins, Cytoskeleton, gamma-Aminobutyric Acid, Gene Expression Regulation, Membrane Proteins, Actin Cytoskeleton, Microtubules, Movement, Cell Line, Tumor, GABA Plasma Membrane Transport Proteins, Mice, PDZ Domains
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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