ArticleThe Journal of biological chemistry2009
Lipid protein interactions couple protonation to conformation in a conserved cytosolic domain of G protein-coupled receptors.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Interdisciplinary biophysical studies of membrane proteins bacteriorhodopsin and rhodopsin.Biophysical reviews · 2023Review
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- The Molecular Switching Mechanism at the Conserved D(E)RY Motif in Class-A GPCRs.Biophysical journal · 2016Article
- SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. I. VIBRATIONAL AND ELECTRONIC SPECTROSCOPY.Optics and spectroscopy · 2015Article
- Fluorescence spectroscopy of rhodopsins: insights and approaches.Biochimica et biophysica acta · 2014Review
- GPCR activation: protonation and membrane potential.Protein & cell · 2013Review
- The swipe card model of odorant recognition.Sensors (Basel, Switzerland) · 2012Review
- Modulation of the interaction between neurotensin receptor NTS1 and Gq protein by lipid.Journal of molecular biology · 2012Article
- Escaping the flatlands: new approaches for studying the dynamic assembly and activation of GPCR signaling complexes.Trends in pharmacological sciences · 2011Review
- Article
- Superactive mutants of thromboxane prostanoid receptor: functional and computational analysis of an active form alternative to constitutively active mutants.Cellular and molecular life sciences : CMLS · 2010Article
- Sequential rearrangement of interhelical networks upon rhodopsin activation in membranes: the Meta II(a) conformational substate.Journal of the American Chemical Society · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The visual photoreceptor rhodopsin is a prototypical class I (rhodopsin-like) G protein-coupled receptor. Photoisomerization of the covalently bound ligand 11-cis-retinal leads to restructuring of the cytosolic face of rhodopsin. The ensuing protonation of Glu-134 in the class-conserved D(E)RY motif at the C-terminal end of transmembrane helix-3 promotes the formation of the G protein-activating state. Using transmembrane segments derived from helix-3 of bovine rhodopsin, we show that lipid protein interactions play a key role in this cytosolic "proton switch." Infrared and fluorescence spectroscopic pK(a) determinations reveal that the D(E)RY motif is an autonomous functional module coupling side chain neutralization to conformation and helix positioning as evidenced by side chain to lipid headgroup Foerster resonance energy transfer. The free enthalpies of helix stabilization and hydrophobic burial of the neutral carboxyl shift the side chain pK(a) into the range typical of Glu-134 in photoactivated rhodopsin. The lipid-mediated coupling mechanism is independent of interhelical contacts allowing its conservation without interference with the diversity of ligand-specific interactions in class I G protein-coupled receptors.
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