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Updated: Jun 5, 2026

Detection of Detergent-sensitive Interactions Between Membrane Proteins
Published on: March 7, 2018
Vimentin binds IRAP and is involved in GLUT4 vesicle trafficking
Yohko Hirata1, Toshio Hosaka, Takeo Iwata
1Department of Nutrition and Metabolism, Institute of Health Biosciences, Tokushima University, Tokushima, Japan.
Abstract:
Insulin-responsive aminopeptidase (IRAP) and GLUT4 are two major cargo proteins of GLUT4 storage vesicles (GSVs) that are translocated from a postendosomal storage compartment to the plasma membrane (PM) in response to insulin. The cytoplasmic region of IRAP is reportedly involved in retention of GSVs. In this study, vimentin was identified using the cytoplasmic domain of IRAP as bait. The validity of this interaction was confirmed by pull-down assays and immunoprecipitation in 3T3-L1 adipocytes. In addition, it was shown that GLUT4 translocation to the PM by insulin was decreased in vimentin-depleted adipocytes, presumably due to dispersing GSVs away from the cytoskeleton. These findings suggest that the IRAP binding protein, vimentin, plays an important role in retention of GSVs.
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