ArticleBiophysical journal2006
Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.
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Who cites it
142 citing papers in PubMed, 288 citations in OpenAlex.
- Cardiolipin Modulates the Activity of the Intramembrane Protease GlpG Inducing Membrane Restructuring.Journal of the American Chemical Society · 2026Article
- Membrane properties modulate methane oxidation by particulate methane monooxygenase.The Journal of biological chemistry · 2026Article
- Molecular basis for the regulation of membrane proteins through preferential lipid solvation.Nature chemical biology · 2026Article
- Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026Article
- Systematic membrane thickness variation across cellular organelles revealed by cryo-ET.The Journal of cell biology · 2026Article
- Lipid Metabolism and Trafficking in the Golgi Apparatus.Sub-cellular biochemistry · 2026Review
- Small angle neutron scattering study of rhodopsin oligomerization and G-protein coupling in a physiologically relevant lipid membrane.Biochimica et biophysica acta. Biomembranes · 2025Review
- Bending the rules: curvature's impact on cell biology.BMC biology · 2025Review
- Deep Structural Characterization of Protein-Bound Lipids via Native MS and Ultraviolet Photodissociation.Analytical chemistry · 2025Article
- Higher-order transient membrane protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Hidden water's influence on rhodopsin activation.Biophysical journal · 2024Review
- SMARTINI3 parametrization of multi-scale membrane models via unsupervised learning methods.Scientific reports · 2024Article
- G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024Review
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Membrane homeostasis beyond fluidity: control of membrane compressibility.Trends in biochemical sciences · 2023Review
- What's the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry.Methods (San Diego, Calif.) · 2023Review
- Membrane mediated mechanical stimuli produces distinct active-like states in the AT1 receptor.Nature communications · 2023Article
- Physiological changes in bilayer thickness induced by cholesterol control GPCR rhodopsin function.Biophysical journal · 2023Article
- Regulation of membrane protein structure and function by their lipid nano-environment.Nature reviews. Molecular cell biology · 2023Review
- Effect of Local Stress on Accurate Modeling of Bacterial Outer Membranes Using All-Atom Molecular Dynamics.Journal of chemical theory and computation · 2023Article
82 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
G protein-coupled receptors (GPCRs) are essential components of cellular signaling pathways. They are the targets of many current pharmaceuticals and are postulated to dimerize or oligomerize in cellular membranes in conjunction with their functional mechanisms. We demonstrate using fluorescence resonance energy transfer how association of rhodopsin occurs by long-range lipid-protein interactions due to geometrical forces, yielding greater receptor crowding. Constitutive association of rhodopsin is promoted by a reduction in membrane thickness (hydrophobic mismatch), but also by an increase in protein/lipid molar ratio, showing the importance of interactions extending well beyond a single annulus of boundary lipids. The fluorescence data correlate with the pK(a) for the MI-to-MII transition of rhodopsin, where deprotonation of the retinylidene Schiff base occurs in conjunction with helical movements leading to activation of the photoreceptor. A more dispersed membrane environment optimizes formation of the MII conformation that results in visual function. A flexible surface model explains both the dispersal and activation of rhodopsin in terms of bilayer curvature deformation (strain) and hydrophobic solvation energy. The bilayer stress is related to the lateral pressure profile in terms of the spontaneous curvature and associated bending rigidity. Transduction of the strain energy (frustration) of the bilayer drives protein oligomerization and conformational changes in a coupled manner. Our findings illuminate the physical principles of membrane protein association due to chemically nonspecific interactions in fluid lipid bilayers. Moreover, they yield a conceptual framework for understanding how the tightly regulated lipid compositions of cellular membranes influence their protein-mediated functions.
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