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XB-ART-1185
Invest Ophthalmol Vis Sci 2005 Nov 01;4611:3988-98. doi: 10.1167/iovs.05-0567.
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A role for cytoskeletal elements in the light-driven translocation of proteins in rod photoreceptors.

Peterson JJ , Orisme W , Fellows J , McDowell JH , Shelamer CL , Dugger DR , Smith WC .


Abstract
Light-driven protein translocation is responsible for the dramatic redistribution of some proteins in vertebrate rod photoreceptors. In this study, the involvement of microtubules and microfilaments in the light-driven translocation of arrestin and transducin was investigated. Pharmacologic reagents were applied to native and transgenic Xenopus tadpoles, to disrupt the microtubules (thiabendazole) and microfilaments (cytochalasin D and latrunculin B) of the rod photoreceptors. Quantitative confocal imaging was used to assess the impact of these treatments on arrestin and transducin translocation. A series of transgenic tadpoles expressing arrestin truncations were also created to identify portions of arrestin that enable arrestin to translocate. Application of cytochalasin D or latrunculin B to disrupt the microfilament organization selectively slowed only transducin movement from the inner to the outer segments. Perturbation of the microtubule cytoskeleton with thiabendazole slowed the translocation of both arrestin and transducin, but only in moving from the outer to the inner segments. Transgenic Xenopus expressing fusions of green fluorescent protein (GFP) with portions of arrestin implicates the C terminus of arrestin as an important portion of the molecule for promoting translocation. This C-terminal region can be used independently to promote translocation of GFP in response to light. The results show that disruption of the cytoskeletal network in rod photoreceptors has specific effects on the translocation of arrestin and transducin. These effects suggest that the light-driven translocation of visual proteins at least partially relies on an active motor-driven mechanism for complete movement of arrestin and transducin.

PubMed ID: 16249472
PMC ID: PMC1578685
Article link: Invest Ophthalmol Vis Sci
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: arrb2 gnat1
Antibodies: Gnat1 Ab1

References [+] :
Arikawa, Organization of actin filaments and immunocolocalization of alpha-actinin in the connecting cilium of rat photoreceptors. 1989, Pubmed