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Prog Mol Biol Transl Sci. 2013;118:21-56. doi: 10.1016/B978-0-12-394440-5.00002-4.

True arrestins and arrestin-fold proteins: a structure-based appraisal.

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1
CEA, IRTSV, Laboratoire Biologie à Grande Echelle, F-38054, Grenoble, France.

Abstract

Arrestin-clan proteins are folded alike, a feature responsible for their recent grouping in a single clan. In human, it includes the well-characterized visual and β-arrestins, the arrestin domain-containing proteins (ARRDCs), isoforms of the retromer subunit VPS26, and DSCR3, a protein involved in Down syndrome. A new arrestin-fold-predicted protein, RGP1, described here may join the clan. Unicellular organisms like the yeast Saccharomyces cerevisiae or the amoeba Dictyostelium discoideum harbor VPS26, DSCR3, and RGP1 isoforms as well as arrestin-related trafficking adaptors or ADCs, but true arrestins are missing. Functionally, members of the arrestin clan have generally a scaffolding role in various membrane protein trafficking events. Despite their similar structure, the mechanism of cargo recognition and internalization and the nature of recruited partners differ for the different members. Based on the recent literature, true arrestins (visual and β-arrestins), ARRDCs, and yeast ARTS are the closest from a functional point of view.

[Indexed for MEDLINE]

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