ArticleBiochemistry2014
Assembly of an activated rhodopsin-transducin complex in nanoscale lipid bilayers.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Selection of an ASIC1a-blocking combinatorial antibody that protects cells from ischemic death.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Purification and Characterization of RhoPDE, a Retinylidene/Phosphodiesterase Fusion Protein and Potential Optogenetic Tool from the Choanoflagellate Salpingoeca rosetta.Biochemistry · 2017Article
- Expression, purification, and spectral tuning of RhoGC, a retinylidene/guanylyl cyclase fusion protein and optogenetics tool from the aquatic fungusThe Journal of biological chemistry · 2017Article
- Conformational equilibria of light-activated rhodopsin in nanodiscs.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Article
- Controlled Co-reconstitution of Multiple Membrane Proteins in Lipid Bilayer Nanodiscs Using DNA as a Scaffold.ACS chemical biology · 2015Article
- Crystallization scale preparation of a stable GPCR signaling complex between constitutively active rhodopsin and G-protein.PloS one · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The formation and characterization of an activated complex of the visual pigment rhodopsin and its downstream signaling partner transducin have been the subject of intense focus by several research groups. While the subunit composition of the activated complex is still the subject of some controversy, our laboratory [Xie, G., D'Antona, A. M., Edwards, P. C., Fransen, M., Standfuss, J., Schertler, G. F. X., and Oprian, D. D. (2011) Biochemistry 50, 10399-10407] and that of Ernst et al. [Ernst, O. P., Gramse, V., Kolbe, M., Hofmann, K. P., and Heck, M. (2007) Proc. Natl. Acad. Sci. U.S.A. 104, 10859-10864] find that the two proteins are present in a 1/1 molar ratio. Unfortunately, these data could not distinguish a ratio of 1/1 from ratios of 2/2, 3/3, etc. For this reason, we reinvestigated the issue of stoichiometry of the activated complex, exploiting the ability of Nanodisc lipid bilayers to isolate single molecules of rhodopsin. We show here that the purified complex in Nanodiscs contains an activated rhodopsin with a covalently bound all-trans-retinal chromophore, that transducin has an empty nucleotide-binding pocket, that the isolated complex is active and dissociates upon addition of guanine nucleotide, and that the stoichiometry corresponds to exactly one molecule of rhodopsin and one molecule of transducin.
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