p300 or CBP is required for insulin-stimulated glucose uptake in skeletal muscle and adipocytes

Abstract

Similarly, p300/CBP can acetylate both insulin receptor substrate 1 in Hep1-6 cells (16), and Akt (15) in both HeLa and HEK293T cells, with acetylation of these proteins decreasing their activity. Furthermore, a recent study identifying the p300/CBP-regulated acetylome in mouse embryonic fibroblasts identified a number of proteins known to contribute to GLUT4 exocytic translocation, including myosin 1C and exocyst complex 2 and 3 (18). Importantly, however, none of these studies investigated the relevance of p300/ CBP acetyltransferase activity to insulin action. To this point, p300/CBP are phosphorylated in response to insulin stimulation in HeLa cells, HEK293T cells, and mouse liver (19-21). Moreover, p300/CBP are phosphorylated by Akt, which increases their acetyltransferase activity in a variety of cell types Considered together, these findings suggest that p300/CBP may be an important regulator of insulin signaling to glucose uptake.