The AKT-GSK3β-eIF2Bε signaling module plays a key role in promoting axon regeneration in the adult mammalian central nervous system.

Dual FAK/PYK2 kinase inhibition disrupts GSK3β phosphorylation and may present a new treatment for colorectal cancer in patients carrying APC mutations.

Mass spectroscopy, molecular modeling and/or molecular dynamics simulations reveal how acetylation regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.

Med16 and GSK3b regulate interferon gamma-mediated MHCII expression in macrophages and are required for CD4+ T cell activation.

The kinase AKT acts as a nodal point that coordinates both positive and negative cues to regulate the regeneration of central nervous system axons in adult mice.

A genetic screen in combination with biochemical approaches reveal hijacking of the host β-catenin destruction complex by the parasite T. gondii to reprogram immune gene expression.

Sequential phosphorylation of NDEL1 Ser336/Ser332 by DYRK2 and GSK3β is a novel regulatory step for actin dynamics that contributes to the neurite outgrowth and neuronal arborization in the developing brain.

OPC-specific genetic inhibition of Akt upstream and downstream molecules in the mouse, and simultaneous OPC fate analysis reveal that PTEN-AKT-GSK3b forms a persistent negative signaling pathway for OL development, in parallel with the AKT-mTORC1 pathway.

A biochemical approach using the Wnt pathway as a model system demonstrates a new mechanism for specificity in interconnected signaling networks through scaffold-mediated shielding of bound proteins.

Specific inhibition of cyclin-dependent kinase-like 5 (CDKL5), a kinase linked to a severe neurodevelopmental disorder, demonstrates an important role in the regulation of excitatory hippocampal synapses and synaptic plasticity that was not previously appreciated in rodent knock-out models.