IRR is involved in glucose-induced endocytosis after insulin secretion

Mami Yamaoka; Takeshi Terabayashi; Tomoki Nishioka; Kozo Kaibuchi; Tomohisa Ishikawa; Toshimasa Ishizaki; Toshihide Kimura

doi:10.1016/j.jphs.2019.07.002

IRR is involved in glucose-induced endocytosis after insulin secretion

Mami Yamaoka, Takeshi Terabayashi, Tomoki Nishioka, Kozo Kaibuchi, Tomohisa Ishikawa, Toshimasa Ishizaki, Toshihide Kimura

Institute for Comprehensive Medical Science

Research output: Contribution to journal › Article › peer-review

Abstract

Endocytosis after insulin secretion plays a pivotal role in the regulation of insulin secretion in pancreatic β-cells. Our recent study suggested that EPI64, a GTPase activating protein for Rab27a, contributes to the regulation of glucose-induced endocytosis, which is mediated by the GDP-bound form of Rab27a. Here, we identified insulin receptor-related receptor (IRR) as an EPI64-interacting protein. Knockdown of IRR inhibited glucose-induced uptake of transferrin, a marker of endocytosis, translocation of the guanine-nucleotide-exchange factor ARNO to the plasma membrane, and generation of phosphatidylinositol 3,4,5-trisphosphate (PIP₃). These results suggest that IRR functions upstream of PIP₃ generation and controls endocytosis after insulin secretion.

Original language	English
Pages (from-to)	300-304
Number of pages	5
Journal	Journal of Pharmacological Sciences
Volume	140
Issue number	3
DOIs	https://doi.org/10.1016/j.jphs.2019.07.002
Publication status	Published - 07-2019

All Science Journal Classification (ASJC) codes

Molecular Medicine
Pharmacology

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title = "IRR is involved in glucose-induced endocytosis after insulin secretion",

abstract = "Endocytosis after insulin secretion plays a pivotal role in the regulation of insulin secretion in pancreatic β-cells. Our recent study suggested that EPI64, a GTPase activating protein for Rab27a, contributes to the regulation of glucose-induced endocytosis, which is mediated by the GDP-bound form of Rab27a. Here, we identified insulin receptor-related receptor (IRR) as an EPI64-interacting protein. Knockdown of IRR inhibited glucose-induced uptake of transferrin, a marker of endocytosis, translocation of the guanine-nucleotide-exchange factor ARNO to the plasma membrane, and generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3). These results suggest that IRR functions upstream of PIP3 generation and controls endocytosis after insulin secretion.",

author = "Mami Yamaoka and Takeshi Terabayashi and Tomoki Nishioka and Kozo Kaibuchi and Tomohisa Ishikawa and Toshimasa Ishizaki and Toshihide Kimura",

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language = "English",

volume = "140",

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journal = "Journal of Pharmacological Sciences",

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T1 - IRR is involved in glucose-induced endocytosis after insulin secretion

AU - Yamaoka, Mami

AU - Terabayashi, Takeshi

AU - Nishioka, Tomoki

AU - Kaibuchi, Kozo

AU - Ishikawa, Tomohisa

AU - Ishizaki, Toshimasa

AU - Kimura, Toshihide

PY - 2019/7

Y1 - 2019/7

N2 - Endocytosis after insulin secretion plays a pivotal role in the regulation of insulin secretion in pancreatic β-cells. Our recent study suggested that EPI64, a GTPase activating protein for Rab27a, contributes to the regulation of glucose-induced endocytosis, which is mediated by the GDP-bound form of Rab27a. Here, we identified insulin receptor-related receptor (IRR) as an EPI64-interacting protein. Knockdown of IRR inhibited glucose-induced uptake of transferrin, a marker of endocytosis, translocation of the guanine-nucleotide-exchange factor ARNO to the plasma membrane, and generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3). These results suggest that IRR functions upstream of PIP3 generation and controls endocytosis after insulin secretion.

AB - Endocytosis after insulin secretion plays a pivotal role in the regulation of insulin secretion in pancreatic β-cells. Our recent study suggested that EPI64, a GTPase activating protein for Rab27a, contributes to the regulation of glucose-induced endocytosis, which is mediated by the GDP-bound form of Rab27a. Here, we identified insulin receptor-related receptor (IRR) as an EPI64-interacting protein. Knockdown of IRR inhibited glucose-induced uptake of transferrin, a marker of endocytosis, translocation of the guanine-nucleotide-exchange factor ARNO to the plasma membrane, and generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3). These results suggest that IRR functions upstream of PIP3 generation and controls endocytosis after insulin secretion.

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