A segment corresponding to amino acids Val170-Arg182 of bovine arrestin is capable of binding to phosphorylated rhodopsin

Eur J Biochem. 1994 Nov 15;226(1):87-97. doi: 10.1111/j.1432-1033.1994.tb20029.x.


In retinal rods, photoexcited rhodopsin (R*) is inactivated upon phosphorylation by rhodopsin kinase and the subsequent binding of arrestin. We have studied the structural role of a cationic region of bovine arrestin (Val170-Arg182) using anti-peptide IgGs specifically recognizing this segment and the corresponding oligopeptide. Our results clearly indicate that amino acids Val170-Arg182 are shielded within the arrestin-rhodopsin-complex and very likely belong to a binding domain of arrestin for phosphorylated R*. The purified anti-peptide IgGs strongly reacted with isolated arrestin but did not recognize arrestin when bound to phosphorylated R*. In agreement with these experiments, the oligopeptide Val170-Arg182 was found to compete with arrestin for binding to phosphorylated R*. Increasing concentrations of this peptide caused an oligomerization of phosphorylated rhodopsin when illuminated by white light as well as in the dark. Unphosphorylated rhodopsin did not oligomerize up to a 400-fold molar ratio of peptide/rhodopsin. Limited proteolysis of the phosphorylated carboxy-terminus of rhodopsin with endoproteinase Asp-N caused a significant decrease in the peptide-induced formation of oligomers. Therefore, Val170-Arg182 of bovine arrestin probably interacts with the phosphorylated carboxy-terminus of rhodopsin. The data presented support the proposal of Palczewski et al. (1991c) considering the region Lys163-Arg182 in bovine arrestin to be a possible binding domain for phosphorylated R*.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies
  • Antigens / chemistry
  • Antigens / immunology
  • Antigens / metabolism*
  • Arginine / metabolism*
  • Arrestin
  • Binding, Competitive
  • Cattle
  • Eye Proteins / chemistry
  • Eye Proteins / immunology
  • Eye Proteins / metabolism*
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Structure, Secondary
  • Rhodopsin / metabolism*
  • Valine / metabolism*


  • Antibodies
  • Antigens
  • Arrestin
  • Eye Proteins
  • Rhodopsin
  • Arginine
  • Valine