ArticleBiochemistry2009
Modulation of molecular interactions and function by rhodopsin palmitylation.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- Mechanisms of Rhodopsin-Related Inherited Retinal Degeneration and Pharmacological Treatment Strategies.Cells · 2025Review
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Rhodopsin as a Molecular Target to Mitigate Retinitis Pigmentosa.Advances in experimental medicine and biology · 2022Review
- Thermostability of a recombinant G protein-coupled receptor expressed at high level in mammalian cell culture.Scientific reports · 2020Article
- Lipid Modifications in Cilia Biology.Journal of clinical medicine · 2019Review
- Differentiating between Inactive and Active States of Rhodopsin by Atomic Force Microscopy in Native Membranes.Analytical chemistry · 2019Article
- Investigating the Nanodomain Organization of Rhodopsin in Native Membranes by Atomic Force Microscopy.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Adaptations in rod outer segment disc membranes in response to environmental lighting conditions.Biochimica et biophysica acta. Molecular cell research · 2017Article
- Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Impact of reduced rhodopsin expression on the structure of rod outer segment disc membranes.Biochemistry · 2015Article
- Nanodomain organization of rhodopsin in native human and murine rod outer segment disc membranes.Biochimica et biophysica acta · 2015Article
- Dynamic single-molecule force spectroscopy of rhodopsin in native membranes.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Biochimica et biophysica acta · 2014Review
- Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin.Structure (London, England : 1993) · 2013Article
- Structural, energetic, and mechanical perturbations in rhodopsin mutant that causes congenital stationary night blindness.The Journal of biological chemistry · 2012Article
- Molecular dynamics simulations reveal specific interactions of post-translational palmitoyl modifications with rhodopsin in membranes.Journal of the American Chemical Society · 2012Article
- Membrane-sensitive conformational states of helix 8 in the metabotropic Glu2 receptor, a class C GPCR.PloS one · 2012Article
- Role of membrane integrity on G protein-coupled receptors: Rhodopsin stability and function.Progress in lipid research · 2011Review
- Rod outer segment retinol formation is independent of Abca4, arrestin, rhodopsin kinase, and rhodopsin palmitylation.Investigative ophthalmology & visual science · 2011Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
Rhodopsin is palmitylated at two cysteine residues in its carboxyl terminal region. We have looked at the effects of palmitylation on the molecular interactions formed by rhodopsin using single-molecule force spectroscopy and the function of rhodopsin using both in vitro and in vivo approaches. A knockin mouse model expressing palmitate-deficient rhodopsin was used for live animal in vivo studies and to obtain native tissue samples for in vitro assays. We specifically looked at the effects of palmitylation on the chromophore-binding pocket, interactions of rhodopsin with transducin, and molecular interactions stabilizing the receptor structure. The structure of rhodopsin is largely unperturbed by the absence of palmitate linkage. The binding pocket for the chromophore 11-cis-retinal is minimally altered as palmitate-deficient rhodopsin exhibited the same absorbance spectrum as wild-type rhodopsin. Similarly, the rate of release of all-trans-retinal after light activation was the same both in the presence and absence of palmitylation. Significant differences were observed in the rate of transducin activation by rhodopsin and in the force required to unfold the last stable structural segment in rhodopsin at its carboxyl terminal end. A 1.3-fold reduction in the rate of transducin activation by rhodopsin was observed in the absence of palmitylation. Single-molecule force spectroscopy revealed a 2.1-fold reduction in the normalized force required to unfold the carboxyl terminal end of rhodopsin. The absence of palmitylation in rhodopsin therefore destabilizes the molecular interactions formed in the carboxyl terminal end of the receptor, which appears to hinder the activation of transducin by light-activated rhodopsin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.