Dara Leto

TL;DR: New insights into insulin signalling reveal that phosphorylation events initiated by the insulin receptor regulate key GLUT4 trafficking proteins, including small GTPases, tethering complexes and the vesicle fusion machinery.

TL;DR: It is reported that insulin regulates this process via the G protein RalA, which is present in Glut4 vesicles and interacts with the exocyst in adipocytes, and serves two functions in insulin action: as a cargo receptor for the Myo1c motor, and as a signal for the unification of theExocyst to target Glut3 vesicle to the plasma membrane.

TL;DR: It is suggested that by reducing production of cAMP in adipocytes, IKKε and TBK1 may contribute to the repression of energy expenditure during obesity.

TL;DR: Biochemical analysis and structural modeling establish that UFMylation is a ribosomal modification specialized to facilitate metazoan-specific protein biogenesis at the ER, suggesting that this modification plays a direct role in cotranslational protein translocation into the ER.

TL;DR: It is shown that RalA is regulated by a Ral GAP complex (RGC 1/2) in insulin action and links PI 3-kinase signaling to Ral a activation and Akt phosphorylates the complex and inhibits its function, resulting in increased Ral A activity and glucose uptake.