Microtubule-microtubule sliding and neurite outgrowth in Drosophila is controlled by a Ser/Thr kinase Tricornered via phosphorylation of a 'mitotic' motor protein Pavarotti.

Slow conformational changes after drug binding rationalize selectivity, affinity and long on-target residence time for kinase inhibitors.

First structural view of a substrate-bound PIKK (PI3K-related-kinase) by cryo-EM explains phosphorylation specificity toward a short amino-acid motif shared across the PIKK family and rationalizes PIKK auto-inhibition by regulatory domain.

Phosphorylation of the Wnt receptor LRP6 directly inhibits glycogen synthase kinase-3 by acting as a pseudosubstrate that stabilizes an active conformation of the enzyme, identical to autoinhibition by phosphorylation of its N terminus.

Structural analysis of the HipBST toxin–antitoxin system from E. coli shows how a toxin kinase has been split into two proteins and encodes its own inhibitor.

Characterization of redox-active cysteines illuminates the understudied regulatory mechanisms of brain-selective kinases.

The molecular mechanism of switching between phosphotransferase- and phosphatase-competent states in histidine-kinases has been uncovered, through direct crystallographic observation of bona fide complexes between a histidine-kinase and its response regulator from Bacillus subtilise.

PS1 phosphorylation at Ser367 is the potential hyperactivity-driven culprit of pathogenic change in PS1 conformation in vitro and in vivo.

The bacterial cytolysin synthetase CylM has a eukaryotic lipid kinase fold despite the absence of any clear sequence similarity, and contains adjacent phosphorylation and phosphate elimination active sites and an ordered activation loop in the absence of peptide substrate or regulatory proteins.

The human NimA-related kinases (Neks) recognize divergent substrate motifs, and include Nek10 as a dual-specificity serine/tyrosine kinase, and Nek6, Nek7 and Nek9 as amplifiers of the Plk1 phospho-motif.