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Structure and function of the visual arrestin oligomer.

Publication ,  Journal Article
Hanson, SM; Van Eps, N; Francis, DJ; Altenbach, C; Vishnivetskiy, SA; Arshavsky, VY; Klug, CS; Hubbell, WL; Gurevich, VV
Published in: EMBO J
March 21, 2007

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.

Duke Scholars

Published In

EMBO J

DOI

ISSN

0261-4189

Publication Date

March 21, 2007

Volume

26

Issue

6

Start / End Page

1726 / 1736

Location

England

Related Subject Headings

  • Scattering, Radiation
  • Rhodopsin
  • Protein Binding
  • Phosphorylation
  • Oligodeoxyribonucleotides
  • Mutagenesis, Site-Directed
  • Models, Molecular
  • Microtubules
  • Magnetic Resonance Spectroscopy
  • Light
 

Citation

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Hanson, S. M., Van Eps, N., Francis, D. J., Altenbach, C., Vishnivetskiy, S. A., Arshavsky, V. Y., … Gurevich, V. V. (2007). Structure and function of the visual arrestin oligomer. EMBO J, 26(6), 1726–1736. https://doi.org/10.1038/sj.emboj.7601614
Hanson, Susan M., Ned Van Eps, Derek J. Francis, Christian Altenbach, Sergey A. Vishnivetskiy, Vadim Y. Arshavsky, Candice S. Klug, Wayne L. Hubbell, and Vsevolod V. Gurevich. “Structure and function of the visual arrestin oligomer.EMBO J 26, no. 6 (March 21, 2007): 1726–36. https://doi.org/10.1038/sj.emboj.7601614.
Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, et al. Structure and function of the visual arrestin oligomer. EMBO J. 2007 Mar 21;26(6):1726–36.
Hanson, Susan M., et al. “Structure and function of the visual arrestin oligomer.EMBO J, vol. 26, no. 6, Mar. 2007, pp. 1726–36. Pubmed, doi:10.1038/sj.emboj.7601614.
Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV. Structure and function of the visual arrestin oligomer. EMBO J. 2007 Mar 21;26(6):1726–1736.

Published In

EMBO J

DOI

ISSN

0261-4189

Publication Date

March 21, 2007

Volume

26

Issue

6

Start / End Page

1726 / 1736

Location

England

Related Subject Headings

  • Scattering, Radiation
  • Rhodopsin
  • Protein Binding
  • Phosphorylation
  • Oligodeoxyribonucleotides
  • Mutagenesis, Site-Directed
  • Models, Molecular
  • Microtubules
  • Magnetic Resonance Spectroscopy
  • Light