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C. elegans phototransduction requires a G protein-dependent cGMP pathway and a taste receptor homolog.


ABSTRACT: The eyeless animal C. elegans is able to sense light and engages in phototaxis behavior that is mediated by photoreceptor cells. However, the molecular and cellular mechanisms underlying phototransduction in C. elegans remain largely unclear. By recording the photoreceptor neuron ASJ in wild-type and various mutant worms, we found that phototransduction in ASJ is a G protein-mediated process and requires membrane-associated guanylate cyclases, but not typical phosphodiesterases. In addition, we found that C. elegans phototransduction requires LITE-1, a candidate photoreceptor protein known to be a member of the invertebrate taste receptor family. Our genetic, pharmacological and electrophysiological data suggest a model in which LITE-1 transduces light signals in ASJ via G protein signaling, which leads to upregulation of the second messenger cGMP, followed by opening of cGMP-sensitive CNG channels and stimulation of photoreceptor cells. Our results identify a phototransduction cascade in C. elegans and implicate the function of a 'taste receptor' in phototransduction.

SUBMITTER: Liu J 

PROVIDER: S-EPMC2882063 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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C. elegans phototransduction requires a G protein-dependent cGMP pathway and a taste receptor homolog.

Liu Jie J   Ward Alex A   Gao Jingwei J   Dong Yongming Y   Nishio Nana N   Inada Hitoshi H   Kang Lijun L   Yu Yong Y   Ma Di D   Xu Tao T   Mori Ikue I   Xie Zhixiong Z   Xu X Z Shawn XZ  

Nature neuroscience 20100502 6


The eyeless animal C. elegans is able to sense light and engages in phototaxis behavior that is mediated by photoreceptor cells. However, the molecular and cellular mechanisms underlying phototransduction in C. elegans remain largely unclear. By recording the photoreceptor neuron ASJ in wild-type and various mutant worms, we found that phototransduction in ASJ is a G protein-mediated process and requires membrane-associated guanylate cyclases, but not typical phosphodiesterases. In addition, we  ...[more]

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