Journal
EMBO JOURNAL
Volume 26, Issue 6, Pages 1726-1736Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7601614
Keywords
arrestin; EPR; oligomer; photoreceptor; signaling
Categories
Funding
- NEI NIH HHS [EY05216, R01 EY011500, R01 EY010336, R01 EY005216, EY11500, R37 EY005216, EY10336] Funding Source: Medline
- NIAID NIH HHS [AI58024, R01 AI058024] Funding Source: Medline
- NIGMS NIH HHS [GM70642, R01 GM070642, T32 GM007628, GM07628, R56 GM070642] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available