fyve-dependent endosomal targeting of an arrestin-related protein in amoebafyve-dependent endosomal瞄准arrestin-related蛋白质的变形虫.pdfVIP

FYVE-Dependent Endosomal Targeting of an Arrestin- Related Protein in Amoeba 1,2,3 1¤ 3,4,5 ´ 1,2,3 1,2,3 Dorian Guetta , Karine Langou , Didier Grunwald , Gerard Klein , Laurence Aubry * ` ´ ´ ´ 1 CEA, DSV, iRTSV, Laboratoire de Biochimie et Biophysique des Systemes Integres, Grenoble, France, 2 LBBSI, UMR5092 CNRS, Grenoble, France, 3 Universite Joseph Fourier, Grenoble, France, 4 CEA, DSV, iRTSV, Lab. Transduction du Signal, Grenoble, France, 5 LTS, EMI104 INSERM, Grenoble, France Abstract Background: Visual and b-arrestins are scaffolding proteins involved in the regulation of receptor-dependent intracellular signaling and their trafficking. The arrestin superfamilly includes several arrestin domain-containing proteins and the structurally related protein Vps26. In Dictyostelium discoideum, the arrestin-domain containing proteins form a family of six members, namely AdcA to -F. In contrast to canonical arrestins, Dictyostelium Adc proteins show a more complex architecture, as they possess, in addition to the arrestin core, other domains, such as C2, FYVE, LIM, MIT and SAM, which potentially mediate selective interactions with either lipids or proteins. Methodology and Principal Findings: A detailed analysis of AdcA has been performed. AdcA extends on both sides of the arrestin core, in particular by a FYVE domain which mediates selective interactions with PI(3)P, as disclosed by intrinsic fluorescence measurements and lipid ove