MAU-8 is a Phosducin-like Protein required for G protein signaling in C. elegans

The mau-8(qm57) mutation inhibits the function of GPB-2, a heterotrimeric G protein β subunit, and profoundly affects behavior through the Gαq/Gαo signaling network in C. elegans. mau-8 encodes a nematode Phosducin-like Protein (PhLP), and the qm57 mutation leads to the loss of a predicted phosphory...

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Bibliographic Details
Published inDevelopmental biology Vol. 294; no. 1; pp. 181 - 191
Main Authors Lacoste, Caroline, Barthaux, Véronique, Iborra, Cécile, Seagar, Michael, Erard-Garcia, Madeleine
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.06.2006
Elsevier
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Summary:The mau-8(qm57) mutation inhibits the function of GPB-2, a heterotrimeric G protein β subunit, and profoundly affects behavior through the Gαq/Gαo signaling network in C. elegans. mau-8 encodes a nematode Phosducin-like Protein (PhLP), and the qm57 mutation leads to the loss of a predicted phosphorylation site in the C-terminal domain of PhLP that binds the Gβγ surface implicated in membrane interactions. In developing embryos, MAU-8/PhLP localizes to the cortical region, concentrates at the centrosomes of mitotic cells and remains associated with the germline blastomere. In adult animals, MAU-8/PhLP is ubiquitously expressed in somatic tissues and germline cells. MAU-8/PhLP interacts with the PAR-5/14.3.3 protein and with the Gβ subunit GPB-1. In mau-8 mutants, the disruption of MAU-8/PhLP stabilizes the association of GPB-1 with the microtubules of centrosomes. Our results indicate that MAU-8/PhLP modulates G protein signaling, stability and subcellular location to regulate various physiological functions, and they suggest that MAU-8 might not be limited to the Gαq/Gαo network.
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ISSN:0012-1606
1095-564X
DOI:10.1016/j.ydbio.2006.02.039