Structural Determinants of Arrestin Functions - Progress in Molecular Biology and Translational Science - page 80

8. Sterne-Marr R, Gurevich VV, Goldsmith P, et al. Polypeptide variants of beta-
arrestin and arrestin3. J Biol Chem . 1993;268:15640- 15648.
9. Rapoport B, Kaufman KD, Chazenbalk GD. Cloning of a member of the arrestin fam-
ily from a human thyroid cDNA library. Mol Cell Endocrinol . 1992;84:R39- R43.
10. Craft CM, Whitmore DH, Wiechmann AF. Cone arrestin identified by targeting
expression of a functional family. J Biol Chem . 1994;269:4613 - 4619.
11. Sakuma H, Murakami A, Fujimaki T, Inana G. Isolation and characterization of the
human X-arrestin gene. Gene . 1998;224:87 - 95.
12. Gurevich EV, Gurevich VV. Arrestins: ubiquitous regulators of cellular signaling path-
ways. Genome Biol . 2006;7:236.
13. Gurevich VV, Hanson SM, Song X, Vishnivetskiy SA, Gurevich EV. The functional
cycle of visual arrestins in photoreceptor cells. Prog Retin Eye Res . 2011;30:405 - 430.
14. Gurevich VV, Gurevich EV. The structural basis of arrestin-mediated regulation of
G-protein-coupled receptors. Pharm Ther . 2006;110:465- 502.
15. Xiao K, McClatchy DB, Shukla AK, et al. Functional specialization of beta-
arrestin interactions revealed by proteomic analysis. Proc Natl Acad Sci USA .
2007;104:12011 - 12016.
16. Shinohara T, Dietzschold B, Craft CM, et al. Primary and secondary structure of
bovine retinal S antigen (48-kDa protein). Proc Natl Acad Sci USA . 1987;84:6975 - 6979.
17. Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G. X-ray crystal structure of
arrestin from bovine rod outer segments. Nature . 1998;391:918 - 921.
18. Hirsch JA, Schubert C, Gurevich VV, Sigler PB. The 2.8 A crystal structure of visual
arrestin: a model for arrestin's regulation. Cell . 1999;97:257 - 269.
19. Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. Crystal structure of
beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Trans-
location. Structure . 2001;9:869- 880.
20. Zhan X, Gimenez LE, Gurevich VV, Spiller BW. Crystal structure of arrestin-3 reveals
the basis of the difference in receptor binding between two non-visual subtypes. J Mol
Biol . 2011;406:467 - 478.
21. Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL. Scaffolding functions
of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry . 2002;

41:3321 - 3328.
22. Sutton RB, Vishnivetskiy SA, Robert J, et al. Crystal structure of cone arrestin at 2.3A:
evolution of receptor specificity. J Mol Biol . 2005;354:1069 - 1080.
23. Granzin J, Cousin A, Weirauch M, Schlesinger R, B¨ ldt G, Batra-Safferling R. Crystal
structure of p44, a constitutively active splice variant of visual arrestin. J Mol Biol .
2012;416:611- 618.
24. Gurevich VV, Benovic JL. Cell-free expression of visual arrestin. Truncation mutagen-
esis identifies multiple domains involved in rhodopsin interaction. J Biol Chem .
1992;267:21919 - 21923.
25. Gurevich VV, Benovic JL. Visual arrestin interaction with rhodopsin. Sequential mul-
tisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin.
J Biol Chem . 1993;268:11628- 11638.
26. Gurevich VV, Chen C-Y, Kim CM, Benovic JL. Visual arrestin binding to rhodopsin.
Intramolecular interaction between the basic N terminus and acidic C terminus of
arrestin may regulate binding selectivity. J Biol Chem . 1994;269:8721- 8727.
27. Gurevich VV, Benovic JL. Visual arrestin binding to rhodopsin. Diverse functional
roles of positively charged residues within the phosphorylation-recognition region
of arrestin. J Biol Chem . 1995;270:6010 - 6016.
28. Gurevich VV, Benovic JL. Mechanism of phosphorylation-recognition by visual
arrestin and the transition of arrestin into a high affinity binding state. Mol Pharmacol .
1997;51:161 - 169.