CEA, IRTSV, Laboratoire Biologie à Grande Echelle, F-38054, Grenoble, France.
Prog Mol Biol Transl Sci. 2013;118:21-56. doi: 10.1016/B978-0-12-394440-5.00002-4.
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.
抑制素蛋白家族成员的折叠方式相似，这一特征是导致它们最近被归为同一家族的原因。在人类中，该家族包括特征明确的视觉和β-抑制素蛋白、含有抑制素结构域的蛋白（ARRDCs）、逆转录酶复合物亚基 VPS26 的异构体，以及唐氏综合征相关蛋白 3（DSCR3）。本文中描述的一种新的抑制素折叠预测蛋白 RGP1 可能也属于该家族。像酵母酿酒酵母或变形虫盘基网柄菌这样的单细胞生物也拥有 VPS26、DSCR3 和 RGP1 异构体以及与抑制素相关的转运衔接蛋白或 ADCs，但真正的抑制素蛋白却不存在。从功能上讲，抑制素蛋白家族成员在各种膜蛋白运输事件中通常发挥支架作用。尽管它们的结构相似，但不同成员的货物识别和内化的机制以及募集的伙伴的性质不同。根据最近的文献，从功能角度来看，真正的抑制素（视觉和β-抑制素蛋白）、ARRDCs 和酵母 ARTS 最为接近。
