A high-throughput comparison of substrate specificities of the Src-family kinases Lck and c-Src against a library of proteome-derived phosphorylation sites reveals that Lck has evolved divergent electrostatic features reflecting its involvement in T-cell signaling.
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.
Chemical inhibition of Bub1 shows that the catalytic activity is not required for normal mitotic progression, but it makes chromosome segregation and cell proliferation more sensitive to the effects of the anti-cancer drug Paclitaxel.
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.