Article
- The EMBO Journal (2007) 26, 1726 - 1736
- doi:10.1038/sj.emboj.7601614
Published online: 1 March 2007
Subject Categories:
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
- Department of Pharmacology, Vanderbilt University, Nashville, TN, USA
- Jules Stein Eye Institute and Department of Chemistry and Biochemistry, UCLA, Los Angeles, CA, USA
- Department of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA
- 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
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.
Keywords:
- arrestin,
- EPR,
- oligomer,
- photoreceptor,
- signaling
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