Format

Send to

Choose Destination
J Physiol Paris. 2006 Mar-May;99(2-3):133-9. Epub 2006 Feb 3.

Light-regulated translocation of signaling proteins in Drosophila photoreceptors.

Author information

1
Department of Physiology, The Hebrew University-Hadassah Medical School, P.O. Box 12272, Jerusalem 91120, Israel.

Abstract

Illumination of Drosophila photoreceptor cells induces multi-facet responses, which include generation of the photoreceptor potential, screening pigment migration and translocation of signaling proteins which is the focus of recent extensive research. Translocation of three signaling molecules is covered in this review: (1) Light-dependent translocation of arrestin from the cytosol to the signaling membrane, the rhabdomere, determines the lifetime of activated rhodopsin. Arrestin translocates in PIP3 and NINAC myosin III dependent manner, and specific mutations which disrupt the interaction between arrestin and PIP3 or NINAC also impair the light-dependent translocation of arrestin and the termination of the response to light. (2) Activation of Drosophila visual G protein, DGq, causes a massive and reversible, translocation of the alpha subunit from the signaling membrane to the cytosol, accompanied by activity-dependent architectural changes. Analysis of the translocation and the recovery kinetics of DGq(alpha) in wild-type flies and specific visual mutants indicated that DGq(alpha) is necessary but not sufficient for the architectural changes. (3) The TRP-like (TRPL) but not TRP channels translocate in a light-dependent manner between the rhabdomere and the cell body. As a physiological consequence of this light-dependent modulation of the TRP/TRPL ratio, the photoreceptors of dark-adapted flies operate at a wider dynamic range, which allows the photoreceptors enriched with TRPL to function better in darkness and dim background illumination. Altogether, signal-dependent movement of signaling proteins plays a major role in the maintenance and function of photoreceptor cells.

PMID:
16458490
PMCID:
PMC1995419
DOI:
10.1016/j.jphysparis.2005.12.010
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center