Phototransduction: crystal clear

Ridge, Kevin D.; Abdulaev, N.G.; Sousa, Marcelo C.; Palczewski, Krzysztof

doi:10.1016/s0968-0004(03)00172-5

Cited by 150 publications

(88 citation statements)

References 68 publications

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“…In addition, the existence of rhodopsin dimers and higher oligomers organized into rafts and paracrystals has been demonstrated by transmission electron (TEM) and atomic force microscopy (AFM) in native murine disc membranes [42][43][44]. These data are further reinforced by a semi-empirical model of rhodopsin's supramolecular organization in the native membrane (model IV-V), and its interaction with transducin (a G protein) and arrestin (a regulatory protein) [43][44][45][46]. More recently, crosslinking experiments confirmed the existence of rhodopsin dimers [47].…”

Section: Introductionmentioning

confidence: 93%

The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes

Suda

Filipek

Palczewski

et al. 2004

Molecular Membrane Biology

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SummaryRhodopsin, the prototypical G-protein-coupled receptor, which is densely packed in the disc membranes of rod outer segments, was proposed to function as a monomer. However, a growing body of evidence indicates dimerization and oligomerization of numerous G-protein-coupled receptors, and atomic force microscopy images revealed rows of rhodopsin dimers in murine disc membranes. In this work we demonstrate by electron microscopy of negatively stained samples, blue native-and sodium dodecyl sulphate-polyacrylamide gel electrophoresis, chemical crosslinking, and by proteolysis that native bovine rhodopsin exists mainly as dimers and higher oligomers. These results corroborate the recent findings from atomic force microscopy and molecular modeling on the supramolecular structure and packing arrangement of murine rhodopsin dimers.

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Section: Introductionmentioning

confidence: 93%

The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes

Suda

Filipek

Palczewski

et al. 2004

Molecular Membrane Biology

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“…The ensuing hyperpolarization initiates the photoresponse of the photoreceptor neuron. A number of relatively recent reviews of photoreceptor function and photoreceptor PDEs have been published (Ridge et al, 2003;Cote, 2004). In addition to their role in retinal phototransduction, substantial evidence has been presented demonstrating that in avian species at least a functioning photoreceptor cascade including activation of a PDE6 is present in pineal gland, which is known to be able to sense light.…”

Section: F Phosphodiesterase 6 Familymentioning

confidence: 99%

Cyclic Nucleotide Phosphodiesterases: Molecular Regulation to Clinical Use

2006

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“…The ROS is filled with membranous disks housing the phototransduction machinery that converts photon absorption by rhodopsin into changes in neurotransmitter release from specialized ribbon synapses, thus transmitting photosensory information to the visual cortex (Burns and Arshavsky, 2005;Ridge et al, 2003;tom Dieck and Brandstatter, 2006). The ROS disk membrane proteins are embedded in a fluid milieu comprised of polyunsaturated phospholipids that are highly enriched in omega-3 docosahexaenoic acid [DHA,].…”

Section: Introductionmentioning

confidence: 99%

Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments

Mazelova

Ransom

Astuto-Gribble

et al. 2009

Journal of Cell Science

118

108

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The biogenesis of cilia-derived sensory organelles, the photoreceptor rod outer segments (ROS), is mediated by rhodopsin transport carriers (RTCs). The small GTPase Rab8 regulates ciliary targeting of RTCs, but their specific fusion sites have not been characterized. Here, we report that the Sec6/8 complex, or exocyst, is a candidate effector for Rab8. We also show that the Qa-SNARE syntaxin 3 is present in the rod inner segment (RIS) plasma membrane at the base of the cilium and displays a microtubule-dependent concentration gradient, whereas the Qbc-SNARE SNAP-25 is uniformly distributed in the RIS plasma membrane and the synapse. Treatment with omega-3 docosahexaenoic acid [DHA, 22:6(n-3)] causes increased co-immunoprecipitation and colocalization of SNAP-25 and syntaxin 3 at the base of the cilium, which results in the increased delivery of membrane to the ROS. This is particularly evident in propranolol-treated retinas, in which the DHA-mediated increase in SNARE pairing overcomes the tethering block, including dissociation of Sec8 into the cytosol. Together, our data indicate that the Sec6/8 complex, syntaxin 3 and SNAP-25 regulate rhodopsin delivery, probably by mediating docking and fusion of RTCs. We show further that DHA, an essential polyunsaturated fatty acid of the ROS, increases pairing of syntaxin 3 and SNAP-25 to regulate expansion of the ciliary membrane and ROS biogenesis.

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Phototransduction: crystal clear

Cited by 150 publications

References 68 publications

The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes

The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes

Cyclic Nucleotide Phosphodiesterases: Molecular Regulation to Clinical Use

Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments

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