An ordered membrane-cytoskeleton network in squid photoreceptor microvilli

Saibil, Helen R.

doi:10.1016/0022-2836(82)90208-x

Cited by 82 publications

(53 citation statements)

References 38 publications

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“…3). Saibil (22) and Blest et al (23) have shown that these densities are associated with the cytoskeleton of the microvillus. According to Blest et al (23), the cytoskeleton of each microvillus consists of an axial filament of 6-to 11-nm diameter running the length of the microvillus and surrounded by amorphous material and a series of side arms linking the axial complex to the plasma membrane of the microvillus.…”

Section: Discussionmentioning

confidence: 99%

Gene encoding cytoskeletal proteins in Drosophila rhabdomeres.

Matsumoto¹,

Isono²,

Pye³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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The ninaC gene is one of eight nina (neither inactivation nor afterpotential) genes identified from mutations that drastically reduce the amount of rhodopsin in the compound eye of Drosophila melanogaster. The gene has been cytogenetically localized to the 27E-28B region of the second chromosome. NaDodSO4/PAGE analysis of eye proteins of flies carrying one, two, or three copies of the ninaC region shows that two eye-specific proteins of molecular weight 170,000 and 130,000 display a strong dependence on the dosage of the ninaC gene, although the dependence is evident only when the dosage is decreased and not when it is increased. All mutations in the ninaC gene studied to date have pronounced effects on these two polypeptides. These results suggest that the ninaC locus encodes these two polypeptides. Ultrastructural studies show that the polypeptides encoded by ninaC are very likely to be important components of the cytoskeletal structure of rhabdomeral microvilli.Among the many Drosophila melanogaster mutants that have been isolated in this laboratory on the basis of their defects in light-evoked electrical responses of the eye (1, 2) are those with greatly reduced amounts ofthe visual pigment, rhodopsin (2-4). These mutants were isolated on the basis of their defect in the prolonged depolarizing afterpotential (PDA) produced by a bright blue stimulus that photoconverts a substantial net amount of rhodopsin to metarhodopsin (Fig.

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Section: Discussionmentioning

confidence: 99%

Gene encoding cytoskeletal proteins in Drosophila rhabdomeres.

Matsumoto¹,

Isono²,

Pye³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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“…The c~oskeleton is likely to maintain the highly ordered structure of the photoreceptor even under osmotic stress 1161, and might be the reason that diffusion of rhodopsin molecules within the microvillus membrane is largely constrained [ 171. The cytoskeleton has been implicated in the breakdown and reassembly of the photosensory membrane [12,18]. Whether it also has a significant role in the metabolic regeneration of the photopigment or in the tr~sduction process has yet to be investigated.…”

Section: Discussionmentioning

confidence: 99%

A light‐induced modification of a 165 kDa polypeptide in crayfish photoreceptors shown by monoclonal antibodies

Baer¹,

Stieve²

1985

FEBS Letters

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In the compound eye of invertebrate animals phototransduction takes place in a specialized structure built by the visual cells -the photoreceptor. We describe monoclonal antibody binding to a photoreceptor polypeptide of about 165 kDa. As can be concluded from its solubilization properties this polypeptide might be a component of the cytoskeleton of the photoreceptor. Two of the monoclonal antibodies were shown to bind differently to illuminated or non-illuminated photoreceptor preparations. As a result of the differential binding of these two antibodies, we conclude that the 165 kDa polypeptide is modified by illumination. One of the monoclonal antibodies cross-reacts with an unidentified antigen in preparations of bovine rod outer segments. Invertebrate photoreceptor Cytoskeleton Monoclonal antibody Light-induced protein mod@ation

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“…However, few studies have investigated the potential of protein-protein interactions and cytoskeletal coupling as mechanisms of visual pigment alignment. A number of potential molecular interaction mechanisms have been previously suggested to occur within photoreceptor membranes, including: (i) visual pigment dimerization and ordered protein-protein arrays [49,50]; (ii) direct anchoring of visual pigment molecules to a relatively fixed axial microvillar cytoskeleton [51 -53]; and (iii) extracellular tethering of visual pigment molecules across microvillar membranes [53]. Studies of these mechanisms are in their infancy, and in many cases are still contentious.…”

Section: Photoreceptors As Polarization Detectors: Visual Pigment Dimmentioning

confidence: 99%

The molecular basis of mechanisms underlying polarization vision

Roberts

Porter

Cronin

2011

Phil. Trans. R. Soc. B

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The underlying mechanisms of polarization sensitivity (PS) have long remained elusive. For rhabdomeric photoreceptors, questions remain over the high levels of PS measured experimentally. In ciliary photoreceptors, and specifically cones, little direct evidence supports any type of mechanism. In order to promote a greater interest in these fundamental aspects of polarization vision, we examined a varied collection of studies linking membrane biochemistry, protein -protein interactions, molecular ordering and membrane phase behaviour. While initially these studies may seem unrelated to polarization vision, a common narrative emerges. A surprising amount of evidence exists demonstrating the importance of protein -protein interactions in both rhabdomeric and ciliary photoreceptors, indicating the possible long-range ordering of the opsin protein for increased PS. Moreover, we extend this direction by considering how such protein paracrystalline organization arises in all cell types from controlled membrane phase behaviour and propose a universal pathway for PS to occur in both rhabdomeric and cone photoreceptors.

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An ordered membrane-cytoskeleton network in squid photoreceptor microvilli

Cited by 82 publications

References 38 publications

Gene encoding cytoskeletal proteins in Drosophila rhabdomeres.

Gene encoding cytoskeletal proteins in Drosophila rhabdomeres.

A light‐induced modification of a 165 kDa polypeptide in crayfish photoreceptors shown by monoclonal antibodies

The molecular basis of mechanisms underlying polarization vision

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