A four-switch long-range allosteric network controls FGF receptor kinase conformational dynamics as well as activity and is applicable to other receptor tyrosine kinases.

Extracellular signals mediated by the EphB2 receptor tyrosine kinase may access the effectors of fundamental cell functions controlled by MYCBP2.

The recruitment of SH2-containing proteins to Epidermal Growth Factor in cells happens more slowly than predicted by in vitro techniques.

PDGF and FGF signal via distinct intracellular pathways to confer different cellular outcomes during craniofacial development.

EZH2/cMET may serve as biomarkers to stratify chondrosarcoma patients for cMET inhibitor treatment.

pYtags are novel biosensors that can be used to measure the activity of a receptor tyrosine kinase of interest in live cells with high spatiotemporal resolution and are applied to reveal rapid activity dynamics of EGFR/ErbB2 signaling.

Ligand binding induces DDR1 kinase activity through recruitment of DDR1 receptors into signalling clusters in which phosphorylation occurs across different dimers.

A high-throughput technique to characterize the substrate specificities of tyrosine kinases identifies the key features of kinases and substrates that enforce accurate signaling from T cell receptors.

HGF-MET signaling phosphorylates- and PTPRK dephosphorylates ZNRF3 to regulate ZNRF3 internalization, functioning as a rheostat for Wnt signaling.

Targeting ErbB receptor tyrosine kinases modifies neutrophil survival and inflammation across multiple species, and reveals a new use for ErbB therapeutics in resolving inflammatory disease.