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
Language
- eng
Conference Location
- England