AMPA receptors in the synapse turnover by monomer diffusion

Jyoji Morise, Kenichi G. N. Suzuki (), Ayaka Kitagawa, Yoshihiko Wakazono, Kogo Takamiya, Taka A. Tsunoyama, Yuri L. Nemoto, Hiromu Takematsu, Akihiro Kusumi () and Shogo Oka ()
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Jyoji Morise: Kyoto University
Kenichi G. N. Suzuki: Gifu University
Ayaka Kitagawa: Kyoto University
Yoshihiko Wakazono: University of Miyazaki
Kogo Takamiya: University of Miyazaki
Taka A. Tsunoyama: Okinawa Institute of Science and Technology Graduate University (OIST), Onna-son
Yuri L. Nemoto: Okinawa Institute of Science and Technology Graduate University (OIST), Onna-son
Hiromu Takematsu: Kyoto University
Akihiro Kusumi: Kyoto University
Shogo Oka: Kyoto University

Nature Communications, 2019, vol. 10, issue 1, 1-18

Abstract: Abstract The number and subunit compositions of AMPA receptors (AMPARs), hetero- or homotetramers composed of four subunits GluA1–4, in the synapse is carefully tuned to sustain basic synaptic activity. This enables stimulation-induced synaptic plasticity, which is central to learning and memory. The AMPAR tetramers have been widely believed to be stable from their formation in the endoplasmic reticulum until their proteolytic decomposition. However, by observing GluA1 and GluA2 at the level of single molecules, we find that the homo- and heterotetramers are metastable, instantaneously falling apart into monomers, dimers, or trimers (in 100 and 200 ms, respectively), which readily form tetramers again. In the dendritic plasma membrane, GluA1 and GluA2 monomers and dimers are far more mobile than tetramers and enter and exit from the synaptic regions. We conclude that AMPAR turnover by lateral diffusion, essential for sustaining synaptic function, is largely done by monomers of AMPAR subunits, rather than preformed tetramers.

Date: 2019
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DOI: 10.1038/s41467-019-13229-8

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