Advances in Genome Science

Advances in Genome Science

Volume: 1

Changing Views on Living Organisms

Indexed in: EMBASE

Genome science or genomics is essential to advancing knowledge in the fields of biology and medicine. Specifically, researchers learn about the molecular biology behind genetic expression in living ...
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Variations Around the Arrestin Fold

Pp. 352-376 (25)

Laurence Aubry, Dorian Guetta and Gérard Klein


Endocytosis of ligand-activated plasma membrane receptors has been shown to contribute to the regulation of their downstream signaling. β-arrestins interact with the phosphorylated tail of activated receptors and act as scaffolds for the recruitment of adaptor proteins and clathrin, that constitute the machinery used for receptor endocytosis. Visual- and β-arrestins have a two-lobe, immunoglobulin-like, β-strand sandwich structure. The recent resolution of the crystal structure of VPS26, one of the retromer subunits, unexpectedly evidenced an arrestin fold in this protein otherwise unrelated to arrestins. From a functional point of view, VPS26 is involved in the retrograde transport of the mannose 6-P receptor from the endosomes to the trans-Golgi network. In addition to the group of true arrestins and Vps26, mammalian cells harbor a vast repertoire of proteins that are related to arrestins on the basis of their PFAM Nter and Cter arrestin-domains, which are named Arrestin Domain-Containing proteins (ARRDCs). The biological role of ARRDC proteins is still poorly understood. The three subfamilies have been merged into an arrestin-related protein clan.

This paper provides an overall analysis of arrestin clan proteins. The structures and functions of members of the subfamilies are reviewed in mammals and model organisms such as Drosophila, Caenorhabditis, Saccharomyces and Dictyostelium.


Arrestins; Vps26; GPCR; Retromer; Trafficking; Endocytosis.


BGE/OdyCell, Institut de Recherches en Technologies et Sciences pour le Vivant, CEA-Grenoble, 17 avenue des Martyrs, 38054 Grenoble Cedex 9, France.