NDLI: Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin

Content Provider	PubMed Central
Author	Zhuang, Tiandi Chen, Qiuyan Cho, Min-kyu Vishnivetskiy, Sergey A. Iverson, Tina M. Gurevich, Vsevolod V. Sanders, Charles R.
Abstract	Solution NMR spectroscopy of labeled arrestin-1 was used to explore its interactions with dark-state phosphorylated rhodopsin (P-Rh), phosphorylated opsin (P-opsin), unphosphorylated light-activated rhodopsin (Rh), and phosphorylated light-activated rhodopsin (P-Rh). Distinct sets of arrestin-1 elements were seen to be engaged by Rh* and inactive P-Rh, which induced conformational changes that differed from those triggered by binding of P-Rh. Although arrestin-1 affinity for Rh was seen to be low (K D > 150 μM), its affinity for P-Rh (KD ∼80 μM) was comparable to the concentration of active monomeric arrestin-1 in the outer segment, suggesting that P-Rh generated by high-gain phosphorylation is occupied by arrestin-1 under physiological conditions and will not signal upon photo-activation. Arrestin-1 was seen to bind P-Rh* and P-opsin with fairly high affinity (K D of ∼50 and 800 nM, respectively), implying that arrestin-1 dissociation is triggered only upon P-opsin regeneration with 11-cis-retinal, precluding noise generated by opsin activity. Based on their observed affinity for arrestin-1, P-opsin and inactive P-Rh very likely affect the physiological monomer-dimer-tetramer equilibrium of arrestin-1, and should therefore be taken into account when modeling photoreceptor function. The data also suggested that complex formation with either P-Rh* or P-opsin results in a global transition in the conformation of arrestin-1, possibly to a dynamic molten globule-like structure. We hypothesize that this transition contributes to the mechanism that triggers preferential interactions of several signaling proteins with receptor-activated arrestins.
Related Links	http://dx.doi.org/10.1073/pnas.1215176110
Ending Page	947
Page Count	6
Starting Page	942
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	110
Language	English
Publisher	National Academy of Sciences
Publisher Date	2013-01-15
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin.

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Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

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Functional map of arrestin-1 at single amino acid resolution

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Monomeric rhodopsin is the minimal functional unit required for arrestin binding*

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Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin

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