Rhodopsin–transducin heteropentamer: Three-dimensional structure and biochemical characterization
Open accessAbstract
The process of vision is initiated when the G protein-coupled receptor, rhodopsin (Rho), absorbs a photon and transitions to its activated Rho(∗) form. Rho(∗) binds the heterotrimeric G protein, transducin (G(t)) inducing GDP to GTP exchange and G(t) dissociation. Using nucleotide depletion and affinity chromatography, we trapped and purified the resulting nucleotide-free Rho(∗)·G(t) complex. Quantitative SDS-PAGE suggested a 2:1 molar ratio of Rho(∗) to G(t) in the complex and its mass determined by scanning transmission electron microscopy was 221±12kDa. A 21.6Å structure was calculated from projections of negatively stained Rho(∗)·G(t) complexes. The molecular envelope thus determined accommodated two Rho molecules together with one G(t) heterotrimer, corroborating the heteropentameric structure of the Rho(∗)·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 [334]
The Introduction (page not provided) describes rhodopsin dimers in native membranes and a proposed Rho*–Rho functional unit. The Results and Discussion (page not provided) support a complex containing two rhodopsin molecules and one transducin, but do not establish that only one monomer is activated under normal lighting conditions. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe molecular envelope accommodated two rhodopsin molecules and one transducin heterotrimer, indicating that the photoactivated rhodopsin-transducin complex is a heteropentamer.
“The determined molecular envelope accommodated two rhodopsin molecules together with one transducin heterotrimer, indicating a heteropentameric structure for the photoactivated rhodopsin–transducin complex.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [334]
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Jastrzębska, B., Chen, Y., Orban, T., Jin, H., Hofmann, L., & Palczewski, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662684 · Cited by 78 · see citing works
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Self-citationAsymmetry of the rhodopsin dimer in complex with transducin
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“Together with our EM structural data, the results presented here unambiguously demonstrate that after light activation, a single Gt heterotrimer binds to a Rho dimer (21, 31).”
BackgroundMethodInfluentialSelf-citationExploring the free-energy landscape of GPCR activation
Alhadeff, R., Vorobyov, I. V., Yoon, H. W., & Warshel, A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810316115 · Cited by 64 · see citing works
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“Several GPCRs have been solubilized as homodimers in association with a single G-protein including the leukotriene B4 BLT1 (Banères and Parello 2003), D 2 -dopamine (Han et al. 2009), 5-HT 4 (Pellissier et al. 2011), and rhodopsin (Jastrzebska et al. 2011).”
Kevany, B., Tsybovsky, Y., Campuzano, I., Schnier, P., Engel, A., & Palczewski, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520700 · Cited by 48 · see citing works
“We used single particle three-dimensional EM to determine the structure of the peripherin-ROM1 complex to a resolution of 18 Å, similar to studies of the pentameric rhodopsin/G-protein complex and theABC transporter ABCA4 (23, 36).”
MethodInfluentialSelf-citationGPCR: G protein complexes—the fundamental signaling assembly
Jastrzębska, B. (2013) · Amino Acids · doi:10.1007/s00726-013-1593-y · Cited by 49 · see citing works
“Semi-empirical model of the complex formed between light-activated rhodopsin dimer and a G t heterotrimer (a) (Jastrzebska et al. 2011) and a structure of T4L-b 2 AR-Gs complex (b) (Rasmussen et al. 2011b) were fitted into a 3D molecular map derived from EM-single particle reconstructions of…”
From Atomic Structures to Neuronal Functions of G Protein–Coupled Receptors
Palczewski, K., & Orban, T. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062012-170313 · Cited by 44 · see citing works
“Because membranes are integral to GPCR signaling (Inagaki et al. 2012, Jastrzebska et al. 2011a, Kaya et al. 2011), this idea deserves serious consideration.”
BackgroundResultInfluentialSelf-citationPrecision vs Flexibility in GPCR signaling
Elgeti, M., Rose, A., Bartl, F. J., Hildebrand, P. W., Hofmann, K., & Heck, M. (2013) · Journal of the American Chemical Society · doi:10.1021/ja405133k · Cited by 45 · see citing works
The rhodopsin-transducin complex houses two distinct rhodopsin molecules
Jastrzebska, B., Ringler, P., Palczewski, K., & Engel, A. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.02.014 · Cited by 42 · see citing works
“A model of Rho ⁄ Gt previously constructed (Jastrzebska et al., 2011b) was found to fit well to the 3D map of the DSG-crosslinked Rho⁄ Gt-LMNG.”
InfluentialSelf-citationProduction of GPCR and GPCR complexes for structure determination
Maeda, S., & Schertler, G. F. X. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.04.006 · Cited by 41 · see citing works
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“Electron microscopic studies of native purified Rho2$Gt heteropentamer (Jastrzebska et al., 2011) also required changes in the relative orientations of both Ga subunit subdomains to fit into the observed density as well as a slight displacement of the Gta C terminus.”
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Self-citation
- Authors
- Jastrzebska, B., Ringler, P., Lodowski, D. T., Moiseenkova-Bell, V., Golczak, M., Müller, S. A., Palczewski, K., & Engel, A.
- Affiliations
- University of Basel (CH)
- Case Western Reserve University (US)
- Corresponding author
- Palczewski, Krzysztof
- Engel, Andreas
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2011-12
- Volume
- 176
- Issue
- 3
- Pages
- 387-394
- ISSN
- 1047-8477 (ISSN-L)
- PMC
- PMC3210324
- OpenAlex
- W2126839526
- Cited by
- 57
- References
- 39
- Citations by year
- 2025: 1 · 2024: 2 · 2022: 1 · 2021: 2 · 2019: 3 · 2018: 2 · 2017: 6 · 2016: 7 · 2015: 7 · 2014: 4 · 2013: 13 · 2012: 7
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- edoc (University of Basel) (submittedVersion)
- Funders
- National Institutes of Health, Foundation Fighting Blindness (EY008061, EY019718, GM079191, P30EY11373)
- Amgen Inc., and the Swiss National Foundation (3100A0–108299)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- rhodopsin, transducin, G protein-coupled receptors, vision, heterotrimeric G proteins, complex structure, molecular envelope, receptor-G protein interaction
- MeSH terms
- Electrophoresis, Polyacrylamide Gel, Guanosine Diphosphate, Guanosine Triphosphate, Light, Models, Molecular, Protein Binding, Rhodopsin, Transducin, Microscopy, Electron, Transmission, Multiprotein Complexes, Protein Multimerization
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