In vivo imaging of extracellular signal-regulated kinase activity reveals radial ERK activation patterns that are associated with cell cycle progression in the mouse epidermis.

Tight regulation of a central developmental kinase cascade evolved through two key mutations.

Prostaglandin E₂-mediated radial spread of PKA activation, caused by calcium transients, is a novel mode of intercellular communication in living mice.

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.

Lineage transformation in lung cancer is dictated by ERK activity and requires permissive chromatin alterations in the context of targeted therapy resistance.

Applying ancestral sequence reconstruction techniques to protein kinases reveals the mutations that underlie different modes of activation.

Genetic and proteomic analyses reveal that the SPARK kinase, which is a regulator of key life-cycle transitions in the parasite Toxoplasma gondii, complexes with an elongin-like protein to regulate several important AGC-family kinases.

Calcium channel blockers accelerate aortic aneurysm and cause premature aortic rupture in a mouse model of Marfan syndrome through protein kinase C-mediated activation of 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.

An immunofluorescent analysis of 465 protein kinases revealed a substantial role of liquid-liquid phase separation in kinase localization and identified new kinase localizations to mitochondria and other organelles.