Light dependent phosphorylation of rhodopsin by ATP

Kühn, Hermann; Dreyer, William J.

doi:10.1016/0014-5793(72)80002-4

Cited by 321 publications

(107 citation statements)

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“…Phosphorylation of photoexcited rhodopsin [9] has been discussed as a possible mechanism for this accelerated ATP-dependent deactivation [8,10]. A completely different effect of ATP on PDE activity might originate from a lightsensitive, Mg-dependent ATPase of the disc membrane [ 11,121 which is cGMP-sensitive and can be measured by light scattering [12,13].…”

Section: Introductionmentioning

confidence: 99%

ATP can promote activation and deactivation of the rod cGMP‐phosphodiesterase

Kamps

Hofmann

1986

FEBS Letters

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The AT (amplified transient) signal is a flash-induced increase of the near-infrared light scattering from isolated bovine rod outer segments and is interpreted as a monitor of cGMP-phosphodiesterase activation [(1985) FEBS Lett. 188, 15-201. We have investigated the effects of ATP and cyclic GMP on this signal. It has been found that ATP enhances the AT signal, the relative effect being the largest for low photoexcitation (-1 rhodopsin per disc membrane). At a high rhodopsin turnover, which saturates the AT amplitude, the effect of ATP is to accelerate the rise of the signal. ATP can also accelerate the falling phase of the signal. This deactivating effect depends on the simultaneous presence of cyclic GMP. The results indicate that ATP acts on the phosphodiesterase activation cycle, promoting activation as well as deactivation, dependent on cGMP as a cofactor.

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Section: Introductionmentioning

confidence: 99%

ATP can promote activation and deactivation of the rod cGMP‐phosphodiesterase

Kamps

Hofmann

1986

FEBS Letters

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“…Deprotonation of Meta II's Schiff base between the chromophore and opsin appeared to be critical for the activating property of light-exposed rhodopsin (12). A fortuitous discovery, made in the early 1970s, that rhodopsin is phosphorylated (13)(14)(15), has been connected with observations that ATP mediates quenching of phosphodiesterase activity (16,17). The responsible rhodopsin kinase has been purified (18) and cloned (19).…”

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confidence: 99%

G Protein-Coupled Receptor Rhodopsin: A Prospectus

Filipek

Stenkamp

Teller

et al. 2003

Annu. Rev. Physiol.

227

196

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Rhodopsin is a retinal photoreceptor protein of bipartite structure consisting of the transmembrane protein opsin and a light-sensitive chromophore 11-cis-retinal, linked to opsin via a protonated Schiff base. Studies on rhodopsin have unveiled many structural and functional features that are common to a large and pharmacologically important group of proteins from the G protein-coupled receptor (GPCR) superfamily, of which rhodopsin is the best-studied member. In this work, we focus on structural features of rhodopsin as revealed by many biochemical and structural investigations. In particular, the high-resolution structure of bovine rhodopsin provides a template for understanding how GPCRs work. We describe the sensitivity and complexity of rhodopsin that lead to its important role in vision.

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“…The primary event in the first cascade is the binding of transducin to light-activated rhodopsin (metarhodopsin II; Meta II), and that in the second is the binding of rhodopsin kinase (RK) to the same photointermediate resulting in its phosphorylation (2)(3)(4). While the structural requirements for interaction between Meta II and transducin have been investigated extensively, the study of RK-rhodopsin interaction has begun only recently.…”

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confidence: 99%

Structure and function in rhodopsin: Peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase

Creuzenet

et al. 1997

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

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Phosphorylation of light-activated rhodopsin by the retina-specific enzyme, rhodopsin kinase (RK), is the primary event in the initiation of desensitization in the visual system. RK binds to the cytoplasmic face of rhodopsin, and the binding results in activation of the enzyme which then phosphorylates rhodopsin at several serine and threonine residues near the carboxyl terminus. To map the RK binding sites, we prepared two sets of rhodopsin mutants in the cytoplasmic CD and EF loops. In the first set, peptide sequences in both loops were either deleted or replaced by indifferent sequences. In the second set of mutants, the charged amino acids (E134, R135, R147, E239, K245, E247, K248, and E249) were replaced by neutral amino acids in groups of 1-3 per mutant. The deletion and replacement mutants in the CD loop showed essentially no phosphorylation, and they appeared to be defective in binding of RK. Of the mutants in the EF loop, that with a deletion of 13 amino acids, was also defective in binding to RK while the second mutant containing a replacement sequence bound RK but showed a reduction of about 70% in V max for phosphorylation. The mutants containing charged to neutral amino acid replacements in the CD and EF loops were all phosphorylated but to different levels. The charge reversal mutant E134R͞ R135E showed a 50% reduction in V max relative to wild-type rhodopsin. Replacements of charged residues in the EF loop decreased the K m by 5-fold for E239Q and E247Q͞K248L͞ E239Q. In summary, both the CD and EF cytoplasmic loops are intimately involved in binding and interaction of RK with light-activated rhodopsin.Light activation of rhodopsin initiates two biochemical cascades, one leading to visual sensitization and the other to desensitization. The primary event in the first cascade is the binding of transducin to light-activated rhodopsin (metarhodopsin II; Meta II), and that in the second is the binding of rhodopsin kinase (RK) to the same photointermediate resulting in its phosphorylation (2-4). While the structural requirements for interaction between Meta II and transducin have been investigated extensively, the study of RK-rhodopsin interaction has begun only recently. Akhtar and coworkers (5) dissected the action of RK into two distinct steps. The first involved binding to Meta II, which resulted in activation of the enzyme. Catalysis of phosphorylation then followed as a second step. Palczweski et al. (6) compared the activation of RK by a number of rhodopsin derivatives and concluded that the cytoplasmic EF loop was involved in binding to RK. More recently, Weiss and coworkers (7) studied the effects of certain amino acid replacements in cytoplasmic loops AB, CD, and EF and suggested the involvement of all the three loops in phosphorylation by RK.We now report on further characterization of the requirements for the binding of RK to Meta II and catalysis of the phosphorylation reaction. Two sets of mutants in the cytoplasmic loops CD and EF ( Fig. 1) (8) have been studied. In one set, pepti...

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Light dependent phosphorylation of rhodopsin by ATP

Cited by 321 publications

References 11 publications

ATP can promote activation and deactivation of the rod cGMP‐phosphodiesterase

ATP can promote activation and deactivation of the rod cGMP‐phosphodiesterase

G Protein-Coupled Receptor Rhodopsin: A Prospectus

Structure and function in rhodopsin: Peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase

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