AKT/AMPK-mediated phosphorylation of TBC1D4 disrupts the interaction with insulin-regulated aminopeptidase
Samaneh Eickelschulte, Sonja Hartwig, Ben Leiser, Stefan Lehr, Viola Joschko, Manopriya Chokkalingam, Alexandra Chadt, Hadi Al‐Hasani
Abstract
were found to be preferred targets for AMPK. Phosphorylation of TBC1D4 by AKT or AMPK did not alter the intrinsic RabGAP activity, but did disrupt interaction with insulin-regulated aminopeptidase (IRAP), a resident protein of GSVs implicated in GLUT4 trafficking. These findings provide evidence that insulin and contraction may regulate TBC1D4 function primarily by disrupting the recruitment of the RabGAP to GLUT4 vesicles.
Topics & Concepts
PhosphorylationProtein kinase BRabGLUT4AMPKBiochemistryInternal medicineMedicineEndocrinologyInsulinProtein kinase ABiologyInsulin resistanceGTPaseCellular transport and secretionMetabolism, Diabetes, and CancerPancreatic function and diabetes