Light adaptation through phosphoinositide-regulated translocation of drosophila visual arrestin

Seung Jae Lee, Hong Xu, Lin Woo Kang, L. Mario Amzel, Craig Montell

Research output: Contribution to journalArticlepeer-review

91 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)121-132
Number of pages12
Issue number1
StatePublished - Jul 3 2003
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)


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