The ubiquitin ligase c-Cbl preferentially targets unique-region phosphorylated LynA for rapid degradation, regulating its expression and differentially tuning signaling responsiveness in macrophages and mast cells.

Unique biosensor design and protein-engineering enables direct visualization of the active form of Fyn kinase with high specificity, minimal perturbation and shows cellular signaling to be compartmentalized and pulsatile.

The T cell response, especially to weak agonists, is enhanced by acute Csk inhibition.

A high-throughput method to profile tyrosine kinases and phosphotyrosine recognition domains reveals new rules for sequence specificity and maps the effects of mutations on the recognition of tyrosine phosphorylation sites.

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

Epithelial cells coordinate integrin signaling with protrusion via a two-protein module, with one protein defining localization and downstream signaling, the other serving as a phosphorylation switch and providing negative feedback.

Degradation of kinase LynA protects macrophages from activation unless cells sense a receptor-binding pathogen or inflammation

The functional role of novel regulatory mechanism within prototypic oncogenic kinase c-Src is described with particular emphasis on cancer cell migration, invasiveness, oncogenic transformation, and multilevel regulation of Src itself.

The Netrin-1 and ephrin-B2 proteins act synergistically in the developing nervous system.

A novel two-step model for integrin activation primed by Cas during cell migration and spreading on multiple extracellular matrix ligands.