Figure 6.

Simplified schematic representation of GLUT4 traffic to the plasma membrane. GLUT4 containing vesicles (GSVs) interact with several molecules as they are delivered towards the cell periphery, then tethered, docked and fused to the plasma membrane. The GSV docks with the plasma membrane as a complex is formed between VAMP2 on the vesicle and synatxin4 and SNAP23 on the plasma membrane. This complex then facilitates the fusion of the GSV with the plasma membrane. Tyrosine phosphorylation of Munc18c regulates its binding to syntaxin4. The insulin receptor phosphorylates Munc18c at Tyr⁵²¹ while PTP1B dephosphorylates Munc18c in adipocytes, thereby linking insulin signaling directly to SNARE exocytosis. Adapted from [46] with modifications.