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Rho GTPases regulate rhabdom morphology in octopus photoreceptors

Published online by Cambridge University Press:  02 August 2005

ARIA M. MILLER
Affiliation:
Department of Biology, California State University, Dominguez Hills, Carson
TERESA RAMIREZ
Affiliation:
Department of Biology, California State University, Dominguez Hills, Carson
FREDDI I. ZUNIGA
Affiliation:
Department of Chemistry, California State University, Dominguez Hills, Carson
GINA H. OCHOA
Affiliation:
Department of Biology, California State University, Dominguez Hills, Carson
SHAUNTE GRAY
Affiliation:
Department of Biology, California State University, Dominguez Hills, Carson
SHANNON D. KELLY
Affiliation:
Department of Biology, California State University, Dominguez Hills, Carson
BRIAN MATSUMOTO
Affiliation:
Neuroscience Research Institute, University of California, Santa Barbara
LAURA J. ROBLES
Affiliation:
Department of Biology, California State University, Dominguez Hills, Carson

Abstract

In the cephalopod retina, light/dark adaptation is accompanied by a decrease/increase in rhabdom size and redistribution of rhodopsin and retinochrome. Rearrangements in the actin cytoskeleton probably govern changes in rhabdom size by regulating the degradation/formation of rhabdomere microvilli. Photopigment movements may be directed by microtubules present in the outer segment core cytoplasm. We believe that rhodopsin activation by light stimulates Rho and Rac signaling pathways, affecting these cytoskeletal systems and their possible functions in controlling rhabdom morphology and protein movements. In this study, we localized cytoskeletal and signaling proteins in octopus photoreceptors to determine their concurrence between the lighting conditions. We used toxin B from Clostridium difficile to inhibit the activity of Rho/Rac and observed its effect on the location of signaling proteins and actin and tubulin. In both lighting conditions, we found Rho in specific sets of juxtaposed rhabdomeres in embryonic and adult retinas. In the light, Rho and actin were localized along the length of the rhabdomere, but, in the dark, both proteins were absent from a space beneath the inner limiting membrane. Rac colocalized with tubulin in the outer segment core cytoplasm and, like Rho, the two proteins were also absent beneath the inner limiting membrane in the dark. The distribution of actin and Rho was affected by toxin B and, in dark-adapted retinas, actin and Rho distribution was similar to that observed in the light. Our results suggest that the Rho/Rac GTPases are candidates for the regulation of rhabdomere size and protein movements in light-dark-adapted octopus photoreceptors.

Type
Research Article
Copyright
2005 Cambridge University Press

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