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FYVE-dependent endosomal targeting of an arrestin-related protein in amoeba.
Guetta D., Langou K., Grunwald D., Klein G., Aubry L.
PLoS ONE 5, 12 (2010) e15249 - http://www.hal.inserm.fr/inserm-00763406
 (21179207) 
FYVE-dependent endosomal targeting of an arrestin-related protein in amoeba.
Dorian Guetta1, Karine Langou1, Didier Grunwald2, Gérard Klein1, Laurence Aubry () 1
1 :  BBSI - Biochimie et biophysique des systèmes intégrés
http://www-dsv.cea.fr/thema/bbsi/Accueil.htm
CNRS : UMR5092 – CEA : DSV/IRTSV – Université Joseph Fourier - Grenoble I
17 Rue des martyrs 38054 GRENOBLE CEDEX 9
France
2 :  Transduction du Signal : Signalisation Calcique et Phosphorylation
http://www,lyon.inserm.fr/unites/e_104.html
INSERM : E104 – Université Joseph Fourier - Grenoble I – CEA : DSV
17, Rue Des Martyrs 38054 GRENOBLE CEDEX 9
France
ANTE-INSERM U836, équipe 4, Muscles et pathologies
BACKGROUND: Visual and β-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 overlay assays. Localization studies showed an enrichment of tagged- and endogenous AdcA on the rim of early macropinosomes and phagosomes. This vesicular distribution relies on a functional FYVE domain. Our data also show that the arrestin core binds the ADP-ribosylation factor ArfA, the unique amoebal Arf member, in its GDP-bound conformation. SIGNIFICANCE: This work describes one of the 6 arrestin domain-containing proteins of Dictyostelium, a novel and atypical member of the arrestin clan. It provides the basis for a better understanding of arrestin-related protein involvement in trafficking processes and for further studies on the expanding roles of arrestins in eukaryotes.
Sciences du Vivant/Biologie cellulaire
Anglais
1932-6203

Articles dans des revues avec comité de lecture
10.1371/journal.pone.0015249
PLoS ONE
Publisher Public Library of Science
ISSN 1932-6203 
internationale
2010
13/12/2010
5
12
e15249

Amino Acid Sequence – Animals – Antibodies – Monoclonal – Arrestin – Dictyostelium – Endosomes – Green Fluorescent Proteins – Lipids – Mice – Microscopy – Fluorescence – Molecular Sequence Data – Protein Structure – Tertiary – Rabbits – Sequence Homology – Amino Acid – Subcellular Fractions
This work was funded by the Commissariat a' l'Energie Atomique, the Centre National de la Recherche Scientifique and the Universite' Joseph Fourier Grenoble I
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