ID 61364
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La, The Mon Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Yamada, Hiroshi Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences Kaken ID publons researchmap
Seiriki, Sayaka Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Li, Shun-AI Center for Innovative Clinical Medicine, Okayama University Hospital
Fujise, Kenshiro Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Katsumi, Natsuho Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Abe, Tadashi Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
Watanabe, Masami Center for Innovative Clinical Medicine, Okayama University Hospital Kaken ID publons researchmap
Takei, Kohji Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences Kaken ID publons researchmap
Abstract
The activity of AMPA-type glutamate receptor is involved in insulin release from pancreatic β-cells. However, the mechanism and dynamics that underlie AMPA receptor-mediated insulin release in β-cells is largely unknown. Here, we show that AMPA induces internalization of glutamate receptor 2/3 (GluR2/3), AMPA receptor subtype, in the mouse β-cell line MIN6. Immunofluorescence experiments showed that GluR2/3 appeared as fine dots that were distributed throughout MIN6 cells. Intracellular GluR2/3 co-localized with AP2 and clathrin, markers for clathrin-coated pits and vesicles. Immunoelectron microscopy revealed that GluR2/3 was also localized at plasma membrane. Surface biotinylation and immunofluorescence measurements showed that addition of AMPA caused an approximate 1.8-fold increase in GluR2/3 internalization under low-glucose conditions. Furthermore, internalized GluR2 largely co-localized with EEA1, an early endosome marker. In addition, GluR2/3 co-immunoprecipitated with cortactin, a F-actin binding protein. Depletion of cortactin by RNAi in MIN6 cells altered the intracellular distribution of GluR2/3, suggesting that cortactin is involved in internalization of GluR2/3 in MIN6 cells. Taken together, our results suggest that pancreatic β-cells adjust the amount of AMPA-type GluR2/3 on the cell surface to regulate the receptive capability of the cell for glutamate.
Keywords
endocytosis
GluR2
AMPA
cortactin
MIN6
Published Date
2020
Publication Title
Cell Structure and Function
Volume
volume45
Issue
issue2
Publisher
Japan Society for Cell Biology
Start Page
121
End Page
130
ISSN
0386-7196
NCID
AA0060007X
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
Copyright Holders
© 2020 The Author(s)
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DOI
Web of Science KeyUT
Related Url
isVersionOf https://doi.org/10.1247/csf.20020
License
https://creativecommons.org/licenses/by/4.0/