Structure and function of the visual arrestin oligomer.

Journal Article (Journal Article)

A distinguishing feature of rod arrestin is its ability to form oligomers at physiological concentrations. Using visible light scattering, we show that rod arrestin forms tetramers in a cooperative manner in solution. To investigate the structure of the tetramer, a nitroxide side chain (R1) was introduced at 18 different positions. The effects of R1 on oligomer formation, EPR spectra, and inter-spin distance measurements all show that the structures of the solution and crystal tetramers are different. Inter-subunit distance measurements revealed that only arrestin monomer binds to light-activated phosphorhodopsin, whereas both monomer and tetramer bind microtubules, which may serve as a default arrestin partner in dark-adapted photoreceptors. Thus, the tetramer likely serves as a 'storage' form of arrestin, increasing the arrestin-binding capacity of microtubules while readily dissociating to supply active monomer when it is needed to quench rhodopsin signaling.

Full Text

Duke Authors

Cited Authors

  • Hanson, SM; Van Eps, N; Francis, DJ; Altenbach, C; Vishnivetskiy, SA; Arshavsky, VY; Klug, CS; Hubbell, WL; Gurevich, VV

Published Date

  • March 21, 2007

Published In

Volume / Issue

  • 26 / 6

Start / End Page

  • 1726 - 1736

PubMed ID

  • 17332750

Pubmed Central ID

  • PMC1829381

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1038/sj.emboj.7601614


  • eng

Conference Location

  • England