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Cited by 343Neuroscience and Neuropharmacology ResearchMemory and Neural MechanismsGenetics and Neurodevelopmental Disorders

Bidirectional Synaptic Plasticity Regulated by Phosphorylation of Stargazin-like TARPs

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Tomita, Susumu, Stein, Valentin, Stocker, Tim J., Nicoll, Roger A., Bredt, David S.·2005·Neuron
DOI 10.1016/j.neuron.2005.01.009
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Abstract

Synaptic plasticity involves protein phosphorylation cascades that alter the density of AMPA-type glutamate receptors at excitatory synapses; however, the crucial phosphorylated substrates remain uncertain. Here, we show that the AMPA receptor-associated protein stargazin is quantitatively phosphorylated and that stargazin phosphorylation promotes synaptic trafficking of AMPA receptors. Synaptic NMDA receptor activity can induce both stargazin phosphorylation, via activation of CaMKII and PKC, and stargazin dephosphorylation, by activation of PP1 downstream of PP2B. At hippocampal synapses, long-term potentiation and long-term depression require stargazin phosphorylation and dephosphorylation, respectively. These results establish stargazin as a critical substrate in the bidirectional control of synaptic strength, which is thought to underlie aspects of learning and memory.

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  • Members of the TARP family interact with all AMPA receptor subunits and control not only membrane insertion but also lateral redistribution.

    “Of particular interest are members of the TARP family, which interact with all AMPA receptor subunits and control not only membrane insertion but also lateral redistribution (Chen et al. 2000;Tomita et al. 2005; see Blakely and Edwards 2012).”

    From NMDA receptor-dependent long-term potentiation and long-term depression (LTP/LTD). (2012) · cites this paper as Tomita et al. 2005

  • GluA1 phosphorylation directly regulates trafficking, but there are other phosphatase substrates, including PSD-95 and Stargazin, that are also involved in synaptic AMPAR removal during LTD.

    “GluA1 phosphorylation directly regulates trafficking, but there are other phosphatase substrates, including PSD-95 and Stargazin, that are also involved in synaptic AMPAR removal during LTD.”

    From AKAP150-Anchored Calcineurin Regulates Synaptic Plasticity by Limiting Synaptic Incorporation of Ca<sup>2+</sup>-Permeable AMPA Receptors (2012) · cites this paper as Tomita et al., 2005

  • NMDA-cLTD activation of CaN and PP1/2A negatively regulates PSD-95 postsynaptic clustering and binding to Stargazin to promote AMPAR removal.

    “In particular, NMDA-cLTD activation of CaN and PP1/2A negatively regulates PSD-95 postsynaptic clustering and binding to Stargazin to promote AMPAR removal”

    From AKAP150-Anchored Calcineurin Regulates Synaptic Plasticity by Limiting Synaptic Incorporation of Ca<sup>2+</sup>-Permeable AMPA Receptors (2012) · cites this paper as Tomita et al., 2005

  • TARP serines can be phosphorylated by CaMKII.

    “These serines can be phosphorylated by CaMKII (283).”

    From Synaptic memory and CaMKII (2023) · cites this paper as [283]

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Authors
Tomita, S., Stein, V., Stocker, T. J., Nicoll, R. A., & Bredt, D. S.
Affiliations
University of California, San Francisco (US)
Corresponding author
Bredt, David S.
ORCID
Venue
Neuron
Publisher
Elsevier BV
Published
2005-01
Volume
45
Issue
2
Pages
269-277
ISSN
0896-6273 (ISSN-L)
DOI
10.1016/j.neuron.2005.01.009
OpenAlex
W1964945221
Cited by
343
References
6
Citations by year
2026: 4 · 2025: 4 · 2024: 10 · 2023: 9 · 2022: 11 · 2021: 24 · 2020: 13 · 2019: 11 · 2018: 14 · 2017: 16 · 2016: 13 · 2015: 16 · 2014: 20 · 2013: 22 · 2012: 23
FWCI
9.55
Type
journal article
Language
en
Open access
Licence
Locations
  • Neuron (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords
stargazin, TARP, AMPA receptor trafficking, synaptic plasticity, protein phosphorylation, CaMKII, protein kinase C, protein phosphatase 1, calcineurin, NMDA receptor, long-term potentiation, long-term depression, hippocampus, synaptic efficacy, learning and memory
MeSH terms
Amino Acid Sequence, Animals, Brain, Enzyme Inhibitors, Cricetinae, Hippocampus, Membrane Proteins, Synaptic Transmission, Neuronal Plasticity, Organ Culture Techniques, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinase C, Synapses, Calcium Channels, Receptors, N-Methyl-D-Aspartate, CHO Cells, Conserved Sequence, Long-Term Potentiation, Calcium-Calmodulin-Dependent Protein Kinases, Receptors, AMPA, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2

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