Structure and function of the visual arrestin oligomer.
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.
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Related Subject Headings
- Scattering, Radiation
- Rhodopsin
- Protein Binding
- Phosphorylation
- Oligodeoxyribonucleotides
- Mutagenesis, Site-Directed
- Models, Molecular
- Microtubules
- Magnetic Resonance Spectroscopy
- Light
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Scattering, Radiation
- Rhodopsin
- Protein Binding
- Phosphorylation
- Oligodeoxyribonucleotides
- Mutagenesis, Site-Directed
- Models, Molecular
- Microtubules
- Magnetic Resonance Spectroscopy
- Light