Docking of Syk to FcεRI is enhanced by Lyn but limited in duration by SHIP1
William K. Kanagy, Cédric Cleyrat, Mohamadreza Fazel, Shayna R. Lucero, Marcel P. Bruchez, Keith A. Lidke, Bridget S. Wilson, Diane S. Lidke
Abstract
Kanagy et al. combine biochemical and fluorescence microscopy methods to determine the interplay between positive and negative signaling molecules within the FcεRI signalosome. The results highlight the ability of ITAM-based signaling to respond to various ITAM phosphorylation patterns, Syk binding conformations, and the presence/absence of key regulatory molecules. These molecular mechanisms provide insight into how disparate immunoreceptors can utilize conserved signaling cascades to tailor their cellular outcomes.
Topics & Concepts
SykLYNBiologyPhosphorylationCell biologyCell signalingSignal transductionDocking (animal)Plasma protein bindingBiophysicsComputational biologyProto-oncogene tyrosine-protein kinase SrcTyrosine kinaseMedicineNursingMast cells and histamineMonoclonal and Polyclonal Antibodies ResearchPI3K/AKT/mTOR signaling in cancer