AI Article Synopsis
- Insulin-responsive aminopeptidase (IRAP) and GLUT4 are crucial proteins involved in the movement of GLUT4 storage vesicles (GSVs) to the cell surface in response to insulin.
- The study identified vimentin as a protein that interacts with the cytoplasmic region of IRAP, supporting the idea that IRAP helps keep GSVs in place.
- Vimentin depletion in adipocytes led to reduced GLUT4 translocation to the plasma membrane, indicating that vimentin is key for maintaining GSV retention near the cytoskeleton.
Article 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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| http://dx.doi.org/10.1016/j.bbrc.2010.12.134 | DOI Listing |
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