Document Detail

Drosophila visual transduction.
MedLine Citation:
PMID:  22498302     Owner:  NLM     Status:  MEDLINE    
Visual transduction in the Drosophila compound eye functions through a pathway that couples rhodopsin to phospholipase C (PLC) and the opening of transient receptor potential (TRP) channels. This cascade differs from phototransduction in mammalian rods and cones, but is remarkably similar to signaling in mammalian intrinsically photosensitive retinal ganglion cells (ipRGCs). In this review, I focus on recent advances in the fly visual system, including the discovery of a visual cycle and insights into the machinery and mechanisms involved in generating a light response in photoreceptor cells.
Craig Montell
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Review     Date:  2012-04-10
Journal Detail:
Title:  Trends in neurosciences     Volume:  35     ISSN:  1878-108X     ISO Abbreviation:  Trends Neurosci.     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-06-04     Completed Date:  2012-10-23     Revised Date:  2014-09-15    
Medline Journal Info:
Nlm Unique ID:  7808616     Medline TA:  Trends Neurosci     Country:  England    
Other Details:
Languages:  eng     Pagination:  356-63     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
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MeSH Terms
Drosophila / physiology*
Drosophila Proteins / metabolism*
Models, Neurological*
Photoreceptor Cells, Invertebrate / physiology*
Rhodopsin / metabolism*
Transient Receptor Potential Channels / metabolism*
Type C Phospholipases / metabolism*
Vision, Ocular / physiology*
Grant Support
R01 EY008117/EY/NEI NIH HHS; R01 EY008117-23/EY/NEI NIH HHS; R01 EY010852/EY/NEI NIH HHS; R01 EY010852-18/EY/NEI NIH HHS
Reg. No./Substance:
0/Drosophila Proteins; 0/TRPgamma protein, Drosophila; 0/Transient Receptor Potential Channels; 9009-81-8/Rhodopsin; EC 3.1.4.-/Type C Phospholipases

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