Makoto Kanzaki

TL;DR: In this article, a yeast two-hybrid library using the amino-terminal region of CAP and identified the caveolar protein flotillin was used to identify a molecular mechanism underlying this subcellular redistribution.

TL;DR: It is shown that phosphorylated Cbl recruits the CrkII–C3G complex to lipid rafts, where C3G specifically activates the small GTP-binding protein TC10, which is essential for insulin-stimulated glucose uptake and GLUT4 translocation.

TL;DR: The combined efforts of numerous research groups employing a range of experimental approaches has led to a clearer molecular picture of how insulin regulates the membrane trafficking of GLUT4.

TL;DR: This channel, which is named growth-factor-regulated channel (GRC), belongs to the TRP-channel family and localizes mainly to intracellular pools under basal conditions and augments calcium entry through GRC by regulating trafficking of the channel.

TL;DR: In vivo time-lapse confocal fluorescent microscopy of actin-yellow fluorescent protein demonstrated that insulin stimulation initially results in cortical actin remodeling followed by an increase in polymerized actin in the peri-nuclear region, and insulin stimulation of cortex actin rearrangements was completely blocked by treatment of the cells with latrunculin B, C. difficile toxin B, and jasplakinolide.