TY - JOUR
T1 - The G-protein beta-subunit GPB-2 in Caenorhabditis elegans regulates the G(o)alpha-G(q)alpha signaling network through interactions with the regulator of G-protein signaling proteins EGL-10 and EAT-16
AU - van der Linden, A.M.
AU - Simmer, F.
AU - Cuppen, E.
AU - Plasterk, R.
N1 - Reporting year: 2001
Metis note: 11333232
PY - 2001
Y1 - 2001
N2 - The genome of Caenorhabditis elegans harbors two genes for G-protein beta-subunits. Here, we describe the characterization of the second G-protein beta-subunit gene gpb-2. In contrast to gpb-1, gpb-2 is not an essential gene even though, like gpb-1, gpb-2 is expressed during development, in the nervous system, and in muscle cells. A loss-of-function mutation in gpb-2 produces a variety of behavioral defects, including delayed egg laying and reduced pharyngeal pumping. Genetic analysis shows that GPB-2 interacts with the GOA-1 (homologue of mammalian G(o)alpha) and EGL-30 (homologue of mammalian G(q)alpha) signaling pathways. GPB-2 is most similar to the divergent mammalian Gbeta5 subunit, which has been shown to mediate a specific interaction with a Ggamma-subunit-like (GGL) domain of RGS proteins. We show here that GPB-2 physically and genetically interacts with the GGL-containing RGS proteins EGL-10 and EAT-16. Taken together, our results suggest that GPB-2 works in concert with the RGS proteins EGL-10 and EAT-16 to regulate GOA-1 (G(o)alpha) and EGL-30 (G(q)alpha) signaling.
AB - The genome of Caenorhabditis elegans harbors two genes for G-protein beta-subunits. Here, we describe the characterization of the second G-protein beta-subunit gene gpb-2. In contrast to gpb-1, gpb-2 is not an essential gene even though, like gpb-1, gpb-2 is expressed during development, in the nervous system, and in muscle cells. A loss-of-function mutation in gpb-2 produces a variety of behavioral defects, including delayed egg laying and reduced pharyngeal pumping. Genetic analysis shows that GPB-2 interacts with the GOA-1 (homologue of mammalian G(o)alpha) and EGL-30 (homologue of mammalian G(q)alpha) signaling pathways. GPB-2 is most similar to the divergent mammalian Gbeta5 subunit, which has been shown to mediate a specific interaction with a Ggamma-subunit-like (GGL) domain of RGS proteins. We show here that GPB-2 physically and genetically interacts with the GGL-containing RGS proteins EGL-10 and EAT-16. Taken together, our results suggest that GPB-2 works in concert with the RGS proteins EGL-10 and EAT-16 to regulate GOA-1 (G(o)alpha) and EGL-30 (G(q)alpha) signaling.
M3 - Article
SN - 0016-6731
VL - 158
SP - 221
EP - 235
JO - Genetics
JF - Genetics
IS - 1
ER -