Vimentin binds IRAP and is involved in GLUT4 vesicle trafficking

• Published in: Biochemical and biophysical research communications Vol. 405; no. 1; pp. 96 - 101
• Main Authors: Hirata, Yohko, Hosaka, Toshio, Iwata, Takeo, Le, Chung T.K., Jambaldorj, Bayasgalan, Teshigawara, Kiyoshi, Harada, Nagakatsu, Sakaue, Hiroshi, Sakai, Tohru, Yoshimoto, Katsuhiko, Nakaya, Yutaka
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 04-02-2011
• Subjects: 3T3-L1 Cells; 60 APPLIED LIFE SCIENCES; Animals; Cystinyl Aminopeptidase - metabolism; Cytoplasmic Vesicles - metabolism; Gene Knockdown Techniques; Glucose Transporter Type 4 - metabolism; GLUT4; IMMUNOASSAY; INSULIN; IRAP; MEMBRANES; Mice; MICROTUBULES; Protein Transport; TRANSLOCATION; Vimentin; Vimentin - genetics; Vimentin - metabolism; Vimentin; GLUT4; IRAP
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2010.12.134

► Vimentin is shown to bind to the N-terminus of insulin-responsive aminopeptidase (IRAP), a major cargo protein of GLUT4 vesicles in 3T3-L1 adipocytes. ► GLUT4 translocation to the plasma membrane by insulin is decreased in vimentin-depleted adipocytes. ► An interaction between vimentin and IRAP functions to sequester GLUT4 vesicles to the peri-nuclear region of the cell.
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.