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Vol. 13, No. 14, pp. 1780-1793, July 15, 1999
and Gq in Caenorhabditis elegans: the RGS protein EAT-16 is necessary for Go signaling and regulates Gq activity
1 Howard Hughes Medical Institute (HHMI) and Division of
Biology, California Institute of Technology, Pasadena, California 91125 USA; 2 Department of Molecular Biophysics and Biochemistry,
Yale University, New Haven, Connecticut 06520 USA
To elucidate the cellular role of the heterotrimeric G protein
Go, we have taken a molecular genetic approach in
Caenorhabditis elegans. We screened for suppressors of
activated GOA-1 (Go
) that do not simply decrease its
expression and found mutations in only two genes, sag-1 and
eat-16. Animals defective in either gene display a hyperactive
phenotype similar to that of goa-1 loss-of-function mutants.
Double-mutant analysis indicates that both sag-1 and
eat-16 act downstream of, or parallel to, Go and negatively regulate EGL-30 (Gq) signaling. eat-16
encodes a regulator of G protein signaling (RGS) most similar to the
mammalian RGS7 and RGS9 proteins and can inhibit endogenous mammalian
Gq/G11 in COS-7 cells. Animals
defective in both sag-1 and eat-16 are inviable, but
reducing function in egl-30 restores viability, indicating that
the lethality of the eat-16; sag-1 double mutant is due
to excessive Gq activity. Analysis of these mutations indicates that the Go and Gq pathways function
antagonistically in C. elegans, and that Go
negatively regulates the Gq pathway, possibly via EAT-16 or
SAG-1. We propose that a major cellular role of Go is to
antagonize signaling by Gq.
[Key Words: C. elegans; Go protein; Gq protein; RGS protein; signaling; regulation]
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