TY - JOUR
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
N1 - Funding Information:
We thank Dr. Jun-Ichi Miyazaki (Osaka University) for providing the MIN6 cells. We also thank Ms. Saemi Himeno and Ms. Chikako Aramaki (Oita University) for the preparation of some materials, and Ms. Kikumi Shimamura and Ms. Chiharu Abe for secretarial and technical assistance. This work was supported in part by the grant KAKENHI ( 17K09838 , 16H07083 and 18K16239 ), Takeda Science Foundation , Novo Nordisk Pharma , Oita Broadcasting System Cultural Foundation , and Suzuken Memorial Foundation .
Funding Information:
We thank Dr. Jun-Ichi Miyazaki (Osaka University) for providing the MIN6 cells. We also thank Ms. Saemi Himeno and Ms. Chikako Aramaki (Oita University) for the preparation of some materials, and Ms. Kikumi Shimamura and Ms. Chiharu Abe for secretarial and technical assistance. This work was supported in part by the grant KAKENHI (17K09838, 16H07083 and 18K16239), Takeda Science Foundation, Novo Nordisk Pharma, Oita Broadcasting System Cultural Foundation, and Suzuken Memorial Foundation.
Publisher Copyright:
© 2019 The Authors
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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U2 - 10.1016/j.jphs.2019.07.002
DO - 10.1016/j.jphs.2019.07.002
M3 - Article
C2 - 31353211
AN - SCOPUS:85071380833
VL - 140
SP - 300
EP - 304
JO - Journal of Pharmacological Sciences
JF - Journal of Pharmacological Sciences
SN - 1347-8613
IS - 3
ER -