Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin
SCIE
SCOPUS
- Title
- Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin
- Authors
- Lee, SJ; Xu, H; Kang, LW; Amzel, LM; Montell, C
- Date Issued
- 2003-07-03
- Publisher
- Cell Press
- Abstract
- Photoreceptor cells adapt to bright or continuous light, although the molecular mechanisms underlying this phenomenon are incompletely understood. Here, we report a mechanism of light adaptation in Drosophila, which is regulated by phosphoinositides (Pis). We found that light-dependent translocation of arrestin was defective in mutants that disrupt PI metabolism or trafficking. Arrestin bound to PIP3 in vitro, and mutation of this site delayed arrestin shuttling and resulted in defects in the termination of the light response, which is normally accelerated by prior exposure to light. Disruption of the arrestin/PI interaction also suppressed retinal degeneration caused by excessive endocytosis of rhodopsin/arrestin complexes. These findings indicate that light-dependent trafficking of arrestin is regulated by direct interaction with Pis and is required for light adaptation. Since phospholipase C activity is required for activation of Drosophila phototransduction, these data point to a dual role of Pis in phototransduction.
- Keywords
- ROD PHOTORECEPTOR CELLS; RECEPTOR ENDOCYTOSIS; PROTEIN; BINDING; PHOTOTRANSDUCTION; GENE; TRP; DEGENERATION; KINASE; DOMAIN
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/27585
- DOI
- 10.1016/S0896-6273(03)00390-8
- ISSN
- 0896-6273
- Article Type
- Article
- Citation
- NEURON, vol. 39, no. 1, page. 121 - 132, 2003-07-03
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.