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Structure and function of the visual arrestin oligomer. EMBO J 2007 Mar 21;26(6):1726-36

Date

03/03/2007

Pubmed ID

17332750

Pubmed Central ID

PMC1829381

DOI

10.1038/sj.emboj.7601614

Scopus ID

2-s2.0-33947577189   84 Citations

Abstract

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.

Author List

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

Author

Candice S. Klug PhD Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Arrestin
Cattle
Crystallization
Humans
Light
Magnetic Resonance Spectroscopy
Microtubules
Models, Molecular
Mutagenesis, Site-Directed
Oligodeoxyribonucleotides
Phosphorylation
Protein Binding
Rhodopsin
Scattering, Radiation
jenkins-FCD Prod-400 0f9a74600e4e79798f8fa6f545ea115f3dd948b2