Conformational Dynamics of Activation for the Pentameric Complex of Dimeric G Protein-Coupled Receptor and Heterotrimeric G Protein
Open accessAbstract
Photoactivation of rhodopsin (Rho), a G protein-coupled receptor, causes conformational changes that provide a specific binding site for the rod G protein, G(t). In this work we employed structural mass spectrometry techniques to elucidate the structural changes accompanying transition of ground state Rho to photoactivated Rho (Rho(∗)) and in the pentameric complex between dimeric Rho(∗) and heterotrimeric G(t). Observed differences in hydroxyl radical labeling and deuterium uptake between Rho(∗) and the (Rho(∗))(2)-G(t) complex suggest that photoactivation causes structural relaxation of Rho following its initial tightening upon G(t) coupling. In contrast, nucleotide-free G(t) in the complex is significantly more accessible to deuterium uptake allowing it to accept GTP and mediating complex dissociation. Thus, we provide direct evidence that in the critical step of signal amplification, Rho(∗) and G(t) exhibit dissimilar conformational changes when they are coupled in the (Rho(∗))(2)-G(t) complex.
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The minimal building block of rhodopsin is a dimer in which only one monomer is activated under normal lighting conditions.
“Physiologically, the minimal building block of rhodopsin is a dimer in which only one monomer is activated under normal lighting conditions”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [333]
The Discussion (page unavailable) says GPCR oligomerization warrants considering at least a dimer and that a single photoactivated rhodopsin can activate transducin. It does not establish that a dimer is rhodopsin’s physiological minimal building block or that only one monomer in each dimer is activated under normal lighting conditions. (LLM, conf=0.84)
Experimental — accuracy not yet measuredUsing structural mass spectrometry, the authors found that the transition from ground-state rhodopsin to its photoactivated state causes a structural relaxation that tightens when transducin binds.
“On the basis of structural mass spectrometry techniques, we found that the transition of ground state rhodopsin to its photoactivated state causes a structural relaxation that then tightens upon transducin binding.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [333]
The Abstract (page not provided) says the authors used structural mass spectrometry and that their measurements suggest rhodopsin relaxes with photoactivation and tightens upon transducin (Gt) coupling. The citing sentence presents that inferred structural sequence as a finding that definitively occurs, omitting the source’s uncertainty. (LLM, conf=0.84)
Experimental — accuracy not yet measuredRhodopsin activation involves geometric cis/trans isomerization of the chromophore, deprotonation of the Schiff linkage, and reorganization of water molecules within the transmembrane domain.
“This activation is accomplished through geometric cis/trans isomerization of the chromophore,182 deprotonation of the Schiff linkage,339 and reorganization of water molecules within the TMD of this receptor.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [333]
Citation 339 follows the claim about deprotonation of the Schiff linkage. The Introduction describes retinal cis-to-trans isomerization, and the Discussion addresses internal water during activation, but no passage in our copy states that the Schiff linkage deprotonates (searched: Schiff, Schiff base deprotonation, protonated Schiff base). (LLM, conf=0.73)
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“More recently, radiolytic footprinting analysis of bound waters revealed that internal water was redistributed when rhodopsin was activated and the rod photoreceptor–specific G protein (transducin or Gt) was subsequently bound (Angel et al. 2009b, Orban et al. 2012b).”
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- Authors
- Orban, T., Jastrzebska, B., Gupta, S., Wang, B., Miyagi, M., Chance, M. R., & Palczewski, K.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Chance, Mark R.
- Palczewski, Krzysztof
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 20
- Issue
- 5
- Pages
- 826-840
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC3351692
- OpenAlex
- W1977314934
- Cited by
- 67
- References
- 74
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 6 · 2016: 10 · 2015: 8 · 2014: 4 · 2013: 17 · 2012: 3
- FWCI
- 4.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Eye Institute (EY-008061, R01EY008061, P30 EY-11373, P30EY011373)
- National Institute of General Medical Sciences (GM 079191, R01GM079191)
- National Institute of Biomedical Imaging and Bioengineering (EB09688, R01EB009688, P30EB09998, P30EB009998)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Keywords
- rhodopsin, G protein-coupled receptors, photoactivation, receptor-G protein complex, conformational dynamics, structural mass spectrometry, deuterium absorption, GTP binding, signal amplification, structural relaxation
- MeSH terms
- Animals, Binding Sites, Cattle, Light, Models, Molecular, Protein Conformation, Rhodopsin, Heterotrimeric GTP-Binding Proteins, Receptors, G-Protein-Coupled, Protein Multimerization
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