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.

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.

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.

AXL enables the priming of the antiviral adaptive immune response by limiting the production of type I interferons in dendritic cells.

Single-molecule immunoprecipitation method reveals that the high catalytic rate and multi-tasking capability make a concerted contribution to the strong signaling potency of the HER2-HER3 heterodimers.

Two cancer related proteins, tyrosine phosphatase PTPRK and ubiquitin ligase ZNRF3, interact to downregulate Wnt receptors, thereby regulating Spemann organizer function during Xenopus development.

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

Signaling by TAM receptor tyrosine kinases requires the coincident engagement of a TAM ligand with both its receptor and the phospholipid phosphatidylserine.

Comparative structural studies reveal how the cytoplasmic tails of Eph receptors can differentiate different downstream target proteins via highly specific SAM–SAM domain interactions.