Article

  • The EMBO Journal (2007) 26, 1726 - 1736
  • doi:10.1038/sj.emboj.7601614

Published online: 1 March 2007

Structure and function of the visual arrestin oligomer

Susan M Hanson1,a, Ned Van Eps2,a, Derek J Francis3, Christian Altenbach2, Sergey A Vishnivetskiy1, Vadim Y Arshavsky4, Candice S Klug3, Wayne L Hubbell2 and Vsevolod V Gurevich1

  1. Department of Pharmacology, Vanderbilt University, Nashville, TN, USA
  2. Jules Stein Eye Institute and Department of Chemistry and Biochemistry, UCLA, Los Angeles, CA, USA
  3. Department of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA
  4. Albert Eye Research Institute, Duke University Medical Center, Durham, NC, USA

Correspondence to:

Vsevolod V Gurevich, Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA. Tel.: +1 615 322 7070; Fax: +1 615 343 6532; E-mail: vsevolod.gurevich@vanderbilt.edu

Wayne L Hubbell, Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA; Tel.: +1 310 206 8830; Fax: +1 310 794 2144; E-mail: hubbellw@jsei.ucla.edu

Candice S Klug, Department of Biophysics, Medical College of Wisconsin, Milwaukee, WI 53226, USA; Tel.: +1 414 456 4015; Fax: +1 414 456 6512; E-mail: candice@mcw.edu

aThese authors contributed equally to this work

Received 22 September 2006; Accepted 26 January 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.

  • Keywords:

    • arrestin,
    • EPR,
    • oligomer,
    • photoreceptor,
    • signaling
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