EFR3 and phosphatidylinositol 4-kinase IIIα regulate insulin-stimulated glucose transport and GLUT4 dispersal in 3T3-L1 adipocytes

Author:

Koester Anna M.12,Geiser Angéline2,Laidlaw Kamilla M.E.1,Morris Silke1,Cutiongco Marie F.A.3,Stirrat Laura2,Gadegaard Nikolaj3,Boles Eckhard4,Black Hannah L.5,Bryant Nia J.5,Gould Gwyn W.12ORCID

Affiliation:

1. 1Institute for Molecular, Cellular and Systems Biology, University of Glasgow, U.K.

2. 2Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, U.K.

3. 3James Watt School of Engineering, University of Glasgow, U.K.

4. 4Institute for Molecular Biosciences, Goethe-University 60438 Frankfurt, Germany

5. 5Department of Biology and York Biomedical Research Institute, University of York, York, U.K.

Abstract

Abstract Insulin stimulates glucose transport in muscle and adipocytes. This is achieved by regulated delivery of intracellular glucose transporter (GLUT4)-containing vesicles to the plasma membrane where they dock and fuse, resulting in increased cell surface GLUT4 levels. Recent work identified a potential further regulatory step, in which insulin increases the dispersal of GLUT4 in the plasma membrane away from the sites of vesicle fusion. EFR3 is a scaffold protein that facilitates localization of phosphatidylinositol 4-kinase type IIIα to the cell surface. Here we show that knockdown of EFR3 or phosphatidylinositol 4-kinase type IIIα impairs insulin-stimulated glucose transport in adipocytes. Using direct stochastic reconstruction microscopy, we also show that EFR3 knockdown impairs insulin stimulated GLUT4 dispersal in the plasma membrane. We propose that EFR3 plays a previously unidentified role in controlling insulin-stimulated glucose transport by facilitating dispersal of GLUT4 within the plasma membrane.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference56 articles.

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