<p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p> <p>To identify novel components in heterotrimeric G-protein signalling, we performed an extensive screen for proteins interacting with <italic>Caenorhabditis elegans</italic>  Gα subunits.
The genome of <italic>C. elegans</italic> contains homologues of each of the four mammalian
classes of Gα subunits (Gs, Gi/o, Gq and G12), and 17 other Gα subunits. We
tested 19 of the GGα subunits and four constitutively activated Gα subunits in a largescale
yeast two-hybrid experiment. This resulted in the identification of 24 clones,
representing 11 different proteins that interact with four different Gα subunits. This
set includes <italic>C. elegans</italic> orthologues of known interactors of Gα subunits, such as
AGS3 (LGN/PINS), CalNuc and Rap1Gap, but also novel proteins, including two
members of the nuclear receptor super family and a homologue of human haspin
(germ cell-specific kinase). All interactions were found to be unique for a specific Gα
subunit but variable for the activation status of the Gα subunit. We used expression
pattern and RNA interference analysis of the G-protein interactors in an attempt
to substantiate the biological relevance of the observed interactions. Furthermore,
by means of a membrane recruitment assay, we found evidence that GPA-7 and the
nuclear receptor NHR-22 can interact in the animal.</p>
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Comp Funct Genomics. 2003 Oct; 4(5):479-491