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PMID: 23277586 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 110 ·No. 3 ·2013-01-15 ·Pages 942-7

Zhuang T, Chen Q, Cho MK, Vishnivetskiy SA, Iverson TM, Gurevich VV, Sanders CR

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 (K(D) ~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.

MeSH Terms
Arrestin/chemistry,genetics,metabolism Binding Sites Humans Kinetics Models, Molecular Multiprotein Complexes/chemistry Mutagenesis, Insertional Nuclear Magnetic Resonance, Biomolecular Opsins/chemistry,metabolism Phosphorylation Photochemical Processes Protein Binding Protein Conformation Protein Interaction Domains and Motifs Recombinant Proteins/chemistry,genetics,metabolism Rhodopsin/chemistry,metabolism
Chemicals
Arrestin Multiprotein Complexes Opsins Recombinant Proteins Rhodopsin
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Zhuang Tiandi
Department of Biochemistry, Center for Structural Biology, Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Chen Qiuyan
Cho Min-Kyu
Vishnivetskiy Sergey A
Iverson Tina M
Gurevich Vsevolod V
Sanders Charles R
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
1091-6490
DOI
10.1073/pnas.1215176110
Published
2013-01-15
Epub
2012-00-31
Pages
942-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC3549108
Subset
IM
Grants
NIGMS NIH HHS · 1R01 GM095633 · United States
NEI NIH HHS · R21 EY018435 · United States
NIGMS NIH HHS · R01 GM077561 · United States
NIGMS NIH HHS · P01 GM080513 · United States
NIGMS NIH HHS · GM077561 · United States
NEI NIH HHS · R01 EY011500 · United States
NIGMS NIH HHS · U54 GM094608 · United States
NIGMS NIH HHS · GM081756 · United States
NEI NIH HHS · 1R21EY018435 · United States
NIGMS NIH HHS · R01 GM095633 · United States
NIGMS NIH HHS · R01 GM081756 · United States
External Links
PubMed source DOI: 10.1073/pnas.1215176110 PMC Full Text View journal details
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