Cover Picture: Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy (ChemBioChem 14/2013)

Abstract

The cover picture shows an artist's view of the phosphorylation–dephosphorylation processes affecting various potential sites (shown as red spheres) of an intrinsically disordered protein domain in the cytoplasm of living cells. The article by A. R. Nebreda, M. Pons, et al. on p. 1820 ff. of this issue shows that the phosphorylation pattern of the unique domain of c-Src, a prototypical oncogene, depends on the steady-state balance between the activities of kinases and phosphatases. Intrinsically disordered domains are often found in eukaryotic proteins and are essential regulatory elements that participate in dynamic interactions with other cell components. Post-translation modifications, including phosphorylation (shown as orange spheres in the scheme), are an important part of the regulation process. These processes can be monitored in vivo and in real time by NMR spectroscopy. Xenopus laevis oocytes, into which isotopically labelled protein can be microinjected, are shown in the background.