The arrestin superfamily: cone arrestins are a fourth family

• Published in: FEBS letters Vol. 362; no. 2; pp. 247 - 255
• Main Authors: Craft, Cheryl M., Whitmore, Donald H.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03.04.1995
• Subjects: Adaptive evolution; Amino Acid Sequence; Animals; Antigens - chemistry; Antigens - genetics; Arrestin; Base Sequence; Biological Evolution; Color vision; Conserved Sequence; DNA, Complementary - analysis; DNA, Complementary - chemistry; Eye Proteins - chemistry; Eye Proteins - genetics; G-protein receptor; Humans; Male; Molecular Sequence Data; Retina; Retina - chemistry; Retinal Cone Photoreceptor Cells - chemistry; RNA, Messenger - analysis; RNA, Messenger - chemistry; Sequence Alignment; Xenopus laevis; Adaptive evolution; Retina; Arrestin; Color vision; Xenopus laevis; G-protein receptor
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)00213-S

Arrestins constitute a superfamily of regulatory proteins that down-regulate phosphorylated G-protein membrane receptors, including rod and cone photoreceptors and adrenergic receptors. The potential role of arrestin in color visual processes led us to identify a cDNA encoding a cone-like arrestin in Xenopus laevis, the principle amphibian biological model system. Alignment of 18 deduced amino acid sequences of all known arrestins from both invertebrate and vertebrate species reveals five arrestin families. Further analysis identifies 7 variable and 4 conservative arrestin structural motifs that may identify potential functional domains. The adaptive evolutionary relationship of Xenopus cone arrestin to the arrestin gene tree suggests high intrafamily homology and early gene duplication events.