G-protein-coupled receptors (GPCR) mediate a complex network of signalling through interaction with arrestins. A new structure of phosphorylated rhodopsin in complex with visual arrestin reveals insight into arrestin binding to the diverse GPCR proteome.
“Cover image of Cell Volume 170, Number 3 Copyright (2017) reprinted with permission from Elsevier”
DEER spectroscopy by Ned van Eps in the Ernst lab was used to validate the crystal structure of the phosphorylated G-protein-coupled receptor (GPCR) rhodopsin in complex with arrestin. EPR measurements confirmed the location of the C-terminal tail of rhodopsin on a arrestin binding surface in a non-crystallographic environment. GPCRs are among the most important cell surface receptors controlling nearly all of our physiology. Termination of G-protein-mediated signalling by an active GPCR requires both phosphorylation of the receptor and subsequent binding of a protein called arrestin. The recent crystal structure solved by X-ray diffraction using a free-electron laser identified how specific phopshorylation patterns in GPCRs are recognized by arrestin. Read in the full paper published in Cell the significance of these important findings.
