Role of membrane integrity on G protein-coupled receptors: Rhodopsin stability and function |
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Authors: | Jastrzebska Beata Debinski Aleksander Filipek Slawomir Palczewski Krzysztof |
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Affiliation: | a Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4965, USA b University of Warsaw, Faculty of Chemistry, 02-093 Warsaw, Poland |
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Abstract: | Rhodopsin is a prototypical G protein-coupled receptor (GPCR) - a member of the superfamily that shares a similar structural architecture consisting of seven-transmembrane helices and propagates various signals across biological membranes. Rhodopsin is embedded in the lipid bilayer of specialized disk membranes in the outer segments of retinal rod photoreceptor cells where it transmits a light-stimulated signal. Photoactivated rhodopsin then activates a visual signaling cascade through its cognate G protein, transducin or Gt, that results in a neuronal response in the brain. Interestingly, the lipid composition of ROS membranes not only differs from that of the photoreceptor plasma membrane but is critical for visual transduction. Specifically, lipids can modulate structural changes in rhodopsin that occur after photoactivation and influence binding of transducin. Thus, altering the lipid organization of ROS membranes can result in visual dysfunction and blindness. |
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Keywords: | G protein-coupled receptor(s) Rhodopsin Transducin (Gt) Photoreceptor Rod outer segment Membranes Oligomerization Signal transduction Phospholipids Cholesterol Phospholipase A2 |
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