論文

査読有り
2020年8月21日

Internalization of AMPA-type Glutamate Receptor in the MIN6 Pancreatic β-cell Line.

Cell structure and function
  • The Mon La
  • ,
  • Hiroshi Yamada
  • ,
  • Sayaka Seiriki
  • ,
  • Shun-Ai Li
  • ,
  • Kenshiro Fujise
  • ,
  • Natsuho Katsumi
  • ,
  • Tadashi Abe
  • ,
  • Masami Watanabe
  • ,
  • Kohji Takei

45
2
開始ページ
121
終了ページ
130
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1247/csf.20020

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.Key words: endocytosis, GluR2, AMPA, cortactin, MIN6.

リンク情報
DOI
https://doi.org/10.1247/csf.20020
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32581155
ID情報
  • DOI : 10.1247/csf.20020
  • PubMed ID : 32581155

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