Two cell-penetrating peptides that inhibit Ras-ERK signalling and a potent clinically relevant MEK inhibitor block cocaine conditioned place preference and accelerate extinction of cocaine self-administration upon a single administration in mice.
Eps8, a specific effector of oncogenic signaling, organizes the cortical actin cytoskeleton of cancer cells to promote mechanical properties that favor a newly identified mode of confined, adhesion-independent cell migration.
An individual extracellular signal regulates multiple cellular actions through differences in the temporal dynamics of spatially distinct populations of the central signaling enzyme, extracellular-signal regulated kinase.
Phosphoproteomics identifies β-arrestin 2 phosphorylation at Thr383 by MEK as a key step of GPCR-induced Erk½ activation, thus providing new insight into the molecular mechanism underlying β-arrestin-dependent GPCR-operated signaling.
The ERK8 kinase blocks the export of glycosyl-tranferases from the Golgi to the endoplasmic reticulum, and thus subsequent O-glycosylation of proteins that otherwise enhance cell motility and tissue invasion.