Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 20, Issue 17, Pages 3865-3877Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E09-01-0021
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- Deutsche Forschungsgemeinschaft [TR-SFB11]
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G protein-coupled receptors (GPCRs) transduce their signals through trimeric G proteins, inducing guanine nucleotide exchange on their G alpha-subunits; the resulting G alpha-GTP transmits the signal further inside the cell. GoLoco domains present in many proteins play important roles in multiple trimeric G protein-dependent activities, physically binding G alpha-subunits of the G alpha(i/o) class. In most cases GoLoco binds exclusively to the GDP-loaded form of the G alpha-subunits. Here we demonstrate that the poly-GoLoco-containing protein Pins of Drosophila can bind to both GDP- and GTP-forms of Drosophila G alpha(o). We identify Pins GoLoco domain 1 as necessary and sufficient for this unusual interaction with G alpha(o)-GTP. We further pinpoint a lysine residue located centrally in this domain as necessary for the interaction. Our studies thus identify Drosophila Pins as a target of G alpha(o)-mediated GPCR receptor signaling, e. g., in the context of the nervous system development, where G alpha(o) acts downstream from Frizzled and redundantly with G alpha(i) to control the asymmetry of cell divisions.
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