Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer

Gray, Noah W.; Fourgeaud, Lawrence; Huang, Bing; Chen, Jing; Cao, Hong; Oswald, Barbara J.; Hémar, Agnès; McNiven, Mark A.

doi:10.1016/s0960-9822(03)00136-2

Cited by 143Neuroscience and Neuropharmacology ResearchCellular transport and secretionGenetics and Neurodevelopmental Disorders

Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer

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Gray, Noah W., Fourgeaud, Lawrence, Huang, Bing, Chen, Jing, Cao, Hong, Oswald, Barbara J., Hémar, Agnès, McNiven, Mark A.·2003·Current Biology

DOI 10.1016/s0960-9822(03)00136-2

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Abstract

The dynamins comprise a large family of mechanoenzymes known to participate in membrane modeling events. All three conventional dynamin genes (Dyn1, Dyn2, Dyn3) are expressed in mammalian brain and produce more than 27 different dynamin proteins as a result of alternative splicing. Past studies have suggested that Dyn1 participates in specialized neuronal functions such as rapid synaptic vesicle recycling, while Dyn2 may mediate the conventional clathrin-mediated uptake of surface receptors. Currently, the distribution, expression, and function of Dyn3 in neurons, or in any other cell type, are completely undefined. Here, we demonstrate that Dyn1 and Dyn3 localize differentially in the synapse. Dyn1 concentrates within the presynaptic compartment, while Dyn3 localizes to dendritic spine tips. Within the postsynaptic density (PSD), we found Dyn3, but not Dyn1, to be part of a biochemically isolated complex comprised of Homer and metabotropic glutamate receptors. Finally, although dominant-negative Dyn3 did not seem to inhibit receptor endocytosis, overexpression of a specific Dyn3 spliced variant in mature neurons caused a marked remodeling of dendritic spines. These data suggest that Dyn3 is a postsynaptic dynamin and, like its binding partner Homer, plays a significant role in dendritic spine morphogenesis and remodeling.

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Loss of certain cytoskeletal proteins appears to be a common mechanism in AD, PD, and ALS, whereas AD-specific modules are linked to loss of a select group of microtubule and related proteins represented by hubs MAP1B (E-M10) and DNM3 (E-M20).
“Thus, loss of certain cytoskeletal proteins appears to be a common mechanism in AD, PD, and ALS, whereas AD-specific modules are linked to a loss of a select group of microtubule and related proteins represented respectively by hubs MAP1B (E-M10) and DNM3 (E-M20) (Gray et al., 2003; Kawakami et al., 2003).”
From A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer’s Disease (2017) · cites this paper as Gray et al., 2003

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Self-citation
Chained together
Wiedemann, C. G. (2007) · Nature reviews. Neuroscience · doi:10.1038/nrn2270
Differential targeting of dynamin-1 and dynamin-3 to nerve terminals during chronic suppression of neuronal activity
Calabrese, B., & Halpain, S. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.03.016 · Cited by 13 · see citing works

Authors: Gray, N. W., Fourgeaud, L., Huang, B., Chen, J., Cao, H., Oswald, B. J., Hémar, A., & McNiven, M. A.
Affiliations: Mayo Clinic (US)
Centre National de la Recherche Scientifique (FR)
Corresponding author: McNiven, Mark A.
ORCID: Gray, Noah W.
Huang, Bing
Chen, Jing
Cao, Hong
McNiven, Mark A.
Venue: Current Biology
Publisher: Elsevier BV
Published: 2003-03
Volume: 13
Issue: 6
Pages: 510-515
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/s0960-9822(03)00136-2
OpenAlex: W2086499290
Cited by: 143
References: 33
Citations by year: 2026: 1 · 2025: 1 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 1 · 2019: 3 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 5 · 2014: 6 · 2013: 12 · 2012: 8
FWCI: 4.27
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, 3791 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: Current Biology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5t32ns007424-05)
National Institute of Neurological Disorders and Stroke (NS07424)
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 › Genetics › Genetics and Neurodevelopmental Disorders
Keywords: DNM3, postsynaptic density, metabotropic glutamate receptor 5, Homer, dendritic spines, spine morphogenesis, dynamin 1, alternative splicing, receptor internalization, synaptic localization
MeSH terms: Homer Scaffolding Proteins, Amino Acid Sequence, Animals, Carrier Proteins, Dendrites, Microscopy, Fluorescence, Molecular Sequence Data, Neuropeptides, Protein Binding, Synapses, Sequence Homology, Amino Acid, Presynaptic Terminals, Kainic Acid Receptors, Protein Transport, Dynamin I, Dynamin III, Rats

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Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer

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