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Visual arrestins in olfactory pathways of Drosophila and the malaria vector mosquito Anopheles gambiae.


ABSTRACT: Arrestins are important components for desensitization of G protein-coupled receptor cascades that mediate neurotransmission as well as olfactory and visual sensory reception. We have isolated AgArr1, an arrestin-encoding cDNA from the malaria vector mosquito, Anopheles gambiae, where olfaction is critical for vectorial capacity. Analysis of AgArr1 expression revealed an overlap between chemosensory and photoreceptor neurons. Furthermore, an examination of previously identified arrestins from Drosophila melanogaster exposed similar bimodal expression, and Drosophila arrestin mutants demonstrate impaired electrophysiological responses to olfactory stimuli. Thus, we show that arrestins in Drosophila are required for normal olfactory physiology in addition to their previously described role in visual signaling. These findings suggest that individual arrestins function in both olfactory and visual pathways in Dipteran insects; these genes may prove useful in the design of control strategies that target olfactory-dependent behaviors of insect disease vectors.

SUBMITTER: Merrill CE 

PROVIDER: S-EPMC122242 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature

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Visual arrestins in olfactory pathways of Drosophila and the malaria vector mosquito Anopheles gambiae.

Merrill C E CE   Riesgo-Escovar J J   Pitts R J RJ   Kafatos F C FC   Carlson J R JR   Zwiebel L J LJ  

Proceedings of the National Academy of Sciences of the United States of America 20020115 3


Arrestins are important components for desensitization of G protein-coupled receptor cascades that mediate neurotransmission as well as olfactory and visual sensory reception. We have isolated AgArr1, an arrestin-encoding cDNA from the malaria vector mosquito, Anopheles gambiae, where olfaction is critical for vectorial capacity. Analysis of AgArr1 expression revealed an overlap between chemosensory and photoreceptor neurons. Furthermore, an examination of previously identified arrestins from Dr  ...[more]

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