Crystal Structure of Cone Arrestin at 2.3Å: Evolution of Receptor Specificity

Sutton, R. Bryan; Vishnivetskiy, Sergey A.; Robert, J. Justin; Hanson, Susan M.; Raman, Dayanidhi; Knox, Barry E.; Kono, Masahiro; Navarro, Javier; Gurevich, Vsevolod V.

doi:10.1016/j.jmb.2005.10.023

Cited by 164 publications

(212 citation statements)

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“…Although the difference between flexible WT arrestin-3 (19) and conformationally restrained ⌬7 mutant (24) could have contributed to the observed difference in BRET efficiency (Fig. 3, C and D), crystal structures of all vertebrate arrestins (19,(52)(53)(54) suggest that KNC mutant likely retains the conformational flexibility of the parental protein. This BRET-based assay is more quantitative than any used so far for this interaction, allowing us to show that WT arrestin-3 and 3A mutant comparably bind JNK3, whereas JNK3 interactions with KNC and especially ⌬7 mutant are significantly stronger (Fig.…”

Section: Discussionmentioning

confidence: 99%

Silent Scaffolds

Breitman

Kook

Giménez

et al. 2012

Journal of Biological Chemistry

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Background: JNK kinases play an important role in cell death and differentiation. Results: Arrestin-3 mutant that binds ASK1, MKK4, and JNK3 normally without promoting JNK3 activation suppresses JNK3 activation in the cell. Conclusion: Modified scaffolding proteins can be used to regulate MAP kinase activity in vivo. Significance: Silent scaffolds are a novel type of molecular tool for manipulation of MAP kinase activity in cells.

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Section: Discussionmentioning

confidence: 99%

Silent Scaffolds

Breitman

Kook

Giménez

et al. 2012

Journal of Biological Chemistry

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“…tains an additional phosphate-binding residue absent in other subtypes (19) and demonstrates the most dramatic phosphorylation-dependent increase in receptor binding in the arrestin family (57,59). As could be expected, WT arrestin-1 better associated with M2R or ␤ 2 AR upon overexpression of GRK2 in COS-7 cells that have a low level of endogenous GRKs ( Fig.…”

Section: Role Of N-terminal Phosphate-binding Element Of Visual Arresmentioning

confidence: 99%

“…The breakdown of the salt bridge between an arginine and aspartic acid in the polar core by charge reversal mutations yielded phosphorylation-independent forms of arrestin-1 (22,29,30,64) and other subtypes (19,(65)(66)(67) that bind active forms of their cognate receptor regardless of their phosphorylation. Two highly exposed lysines in ␤-strand I (Fig.…”

Section: Discusionmentioning

confidence: 99%

Role of Receptor-attached Phosphates in Binding of Visual and Non-visual Arrestins to G Protein-coupled Receptors

Giménez

Kook

Vishnivetskiy

et al. 2012

Journal of Biological Chemistry

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Background:The relative contribution of phosphates and active GPCR conformation is unknown. Results: Using WT and mutant arrestins and receptors, we show that phosphates are critical for arrestin binding to some GPCRs but not to others. Conclusion:The role of receptor-attached phosphates in arrestin binding varies widely depending on the arrestin-receptor combination. Significance: Distinct molecular mechanisms mediate arrestin recruitment to different GPCRs.

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“…It should be noted that the idea of a misfit between the large receptor-binding surface of arrestins and smaller arrestin-binding surface of GPCRs is purely speculative. Many residues on the concave side of the N domain of arrestin-1 directly bind receptor-attached phosphates (7,50). Receptor elements that are phosphorylated are either unresolved or partially resolved [the C termini of rhodopsin (34) and β2-adrenoceptor (51)] or simply deleted [the third cytoplasmic loop of M2 muscarinic receptor (52)] even in the best GPCR crystal structures.…”

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Conformation of receptor-bound visual arrestin

Kim

Vishnivetskiy²,

Eps

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Arrestin-1 (visual arrestin) binds to light-activated phosphorylated rhodopsin (P-Rh*) to terminate G-protein signaling. To map conformational changes upon binding to the receptor, pairs of spin labels were introduced in arrestin-1 and double electron-electron resonance was used to monitor interspin distance changes upon P-Rh* binding. The results indicate that the relative position of the N and C domains remains largely unchanged, contrary to expectations of a "clam-shell" model. A loop implicated in P-Rh* binding that connects β-strands V and VI (the "finger loop," residues 67-79) moves toward the expected location of P-Rh* in the complex, but does not assume a fully extended conformation. A striking and unexpected movement of a loop containing residue 139 away from the adjacent finger loop is observed, which appears to facilitate P-Rh* binding. This change is accompanied by smaller movements of distal loops containing residues 157 and 344 at the tips of the N and C domains, which correspond to "plastic" regions of arrestin-1 that have distinct conformations in monomers of the crystal tetramer. Remarkably, the loops containing residues 139, 157, and 344 appear to have high flexibility in both free arrestin-1 and the P-Rh*complex.A rrestin was first discovered in the visual system as a protein that blocks ("arrests") the signaling of the prototypical G protein-coupled receptor (GPCR) rhodopsin (Rh) via specific binding to the phosphorylated activated form P-Rh* (1). Mammals express four arrestin subtypes: Arrestin-1 and -4 are specific for the visual system, whereas arrestin-2 and -3 are ubiquitous (2). [We use systematic names of arrestins: arrestin-1 (historic names S-antigen, 48-kDa protein, or visual or rod arrestin), arrestin-2 (β-arrestin or β-arrestin1), arrestin-3 (β-arrestin2 or hTHY-ARRX), and arrestin-4 (cone or X-arrestin).] The discovery of nonvisual arrestins (3) showed that phosphorylation followed by arrestin binding is a common mechanism of GPCR regulation. Crystal structures of all four arrestin subtypes in their basal state revealed similar topology: two cup-like domains linked by an interdomain hinge ( Fig. 1) (4-7). Arrestin-1 was proposed to undergo a conformational rearrangement during the P-Rh* interaction that results in the release of the C-terminal sequence (C tail) (8, 9) but does not involve major secondary structure changes (8, 10). Recent site-directed spin labeling (SDSL) studies identified specific parts of arrestin-1 engaged by different functional forms of rhodopsin and provided direct evidence of binding-induced conformational changes (11,12). A conformational change in the so-called finger loop (Fig. 1) implicated in P-Rh* recognition was also observed using NMR and fluorescence quenching (13,14). Arrestin-1 shows a remarkable selectivity for P-Rh*. Observed binding to inactive phosphorylated (P-Rh) or active unphosphorylated rhodopsin (Rh*) is usually less than 10% of the binding to P-Rh*, whereas its binding to inactive unphosphorylated rhodopsin (Rh) is barely detectable ...

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Crystal Structure of Cone Arrestin at 2.3Å: Evolution of Receptor Specificity

Cited by 164 publications

References 56 publications

Silent Scaffolds

Silent Scaffolds

Role of Receptor-attached Phosphates in Binding of Visual and Non-visual Arrestins to G Protein-coupled Receptors

Conformation of receptor-bound visual arrestin

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