Abstract
This review will provide and overview of what is known, and what is not known, about the visual signal termination process in mammalian vision. The focus will be on the role of structure and dynamic changes in the primary mammalian photo-transducer rhodopsin, and the protein that attenuates rhodopsin signaling, arrestin. Although this review focuses on mammalian photoreceptor proteins, analogous mechanisms may be used in the phototransduction pathways of other organisms.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Babu KR, Dukkipati A, Birge RR, Knox BE (2001) Regulation of phototransduction in short-wavelength cone visual pigments via the retinylidene Schiff base counterion. Biochemistry 40: 13760–13766
Borhan B, Souto ML, Imai H, Shichida Y, Nakanishi K (2000) Movement of retinal along the visual transduction path. Science 288: 2209–2212
Dunham TD, Farrens DL (1999) Conformational changes in rhodopsin. Movement of helix F detected by site-specific chemical labeling and fluorescence spectroscopy. J Biol Chem 274: 1683–1690
Ebrey T, Koutalos Y (2001) Vertebrate photoreceptors. Prog Retin Eye Res 20: 49–94
Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274: 768–770
Ghanouni P, Steenhuis JJ, Farrens DL, Kobilka BK (2001) Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor. Proc Natl Acad Sci USA 98: 5997–6002
Gurevich VV, Gurevich EV (2004) The molecular acrobatics of arrestin activation. Trends Pharmacol Sci 25: 105–111
Hubbell WL, Altenbach C, Hubbell CM, Khorana HG (2003) Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv Protein Chem 63: 243–290
Hwa J, Klein-Seetharaman J, Khorana HG (2001) Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proc Natl Acad Sci USA 98: 4872–4876
Janz JM (2004) Structural dynamics of rhodopsin: relationships between retinal Schiff base integrity and receptor signaling states. Oregon Health and Science University, Portland, OR
Janz JM, Farrens DL (2003) Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms. Vis Res 43: 2991–3002
Janz JM, Farrens DL (2004) Rhodopsin activation exposes a key hydrophobic binding site for the transducin alpha-subunit C terminus. J Biol Chem 279: 29767–29773
Klein-Seetharaman J, Getmanova EV, Loewen MC, Reeves PJ, Khorana HG (1999) NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution (19)F NMR. Proc Natl Acad Sci USA 96: 13744–13749
McBee JK, Palczewski K, Baehr W, Pepperberg DR (2001) Confronting complexity: the interlink of phototransduction and retinoid metabolism in the vertebrate retina. Prog Retin Eye Res 20: 469–529
Okada T, Ernst OP, Palczewski K, Hofmann KP (2001) Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem Sci 26: 318–324
Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M (2000) Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289: 739–745
Pulvermuller A, Schroder K, Fischer T, Hofmann KP (2000) Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin. J Biol Chem 275: 37679–37685
Ridge KD, Lu Z, Liu X, Khorana HG (1995) Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons. Biochemistry 34: 3261–3267
Ridge KD, Abdulaev NG, Sousa M, Palczewski K (2003) Phototransduction: crystal clear. Trends Biochem Sci 28: 479–487
Sakamoto T, Khorana HG (1995) Structure and function in rhodopsin: the fate of opsin formed upon the decay of light-activated metarhodopsin II in vitro. Proc Natl Acad Sci USA 92: 249–253
Shilton BH, McDowell JH, Smith WC, Hargrave PA (2002) The solution structure and activation of visual arrestin studied by small-angle X-ray scattering. Eur J Biochem 269: 3801–3809
Smith WC, Hargrave PA (2000) Mapping interaction sites between rhodopsin and arrestin by phage display and synthetic peptides. Methods Enzymol 315: 437–455
Vogel R, Siebert F (2002) Conformation and stability of alpha-helical membrane proteins. 2. Influence of pH and salts on stability and unfolding of rhodopsin. Biochemistry 41: 3536–3545
Xie G, Gross AK, Oprian DD (2003) An opsin mutant with increased thermal stability. Biochemistry 42: 1995–2001
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2005 Yamada Science Foundation and Springer-Verlag Tokyo
About this chapter
Cite this chapter
Farrens, D.L. (2005). Structural Dynamics of the Signal Termination Process in Rhodopsin. In: Wada, M., Shimazaki, Ki., Iino, M. (eds) Light Sensing in Plants. Springer, Tokyo. https://doi.org/10.1007/4-431-27092-2_23
Download citation
DOI: https://doi.org/10.1007/4-431-27092-2_23
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-24002-0
Online ISBN: 978-4-431-27092-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)