Motor proteins transport insulin-containing vesicles toward the membrane (Martin-Urdiroz et al., 2016[83]). This movement is both random and directed along microtubules (Renström and Rorsman, 2007[104]), which are distributed throughout the cell, except in the periphery, where there is an actin web (Renström, 2011[103]). Anterograde (forward) movement of granules depends on kinesin-1 with a maximum velocity of 600-800 nm/sec (Renström and Rorsman, 2007[104]); kinesin-3 may provide a very fast (1000 nm/sec) insulin granule translocation to the plasma membrane (Renström and Rorsman, 2007[104]). As kinesins are ATP-dependent, glucose, by increasing the cytosolic ATP level, increases kinesin activity and therefore insulin secretion (Wang and Thurmond, 2009[129]). Movement of insulin granules in the reverse direction is achieved through dynein (Renström and Rorsman, 2007[104]). Under basal conditions, actin filaments under the plasma membrane prevent insulin hypersecretion (Renström and Rorsman, 2007[104]). However, glucose transiently causes F-actin remodeling, regulated by the small Rho-family GTPases, Cdc42 and Rac1. Cdc42 is activated within 3 minutes of glucose stimulation while Rac1 activation is not apparent until 15-20 minutes after stimulation (Wang and Thurmond, 2009[129]).