Drosophila GoLoco-protein Pins is a target of Galpha(o)-mediated G protein-coupled receptor signaling

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2009
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Molecular biology of the cell. 2009, 20(17), pp. 3865-3877. ISSN 1059-1524. eISSN 1939-4586. Available under: doi: 10.1091/mbc.e09-01-0021
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G protein-coupled receptors (GPCRs) transduce their signals through trimeric G proteins, inducing guanine nucleotide exchange on their Galpha-subunits; the resulting Galpha-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 Galpha-subunits of the Galpha(i/o) class. In most cases GoLoco binds exclusively to the GDP-loaded form of the Galpha-subunits. Here we demonstrate that the poly-GoLoco-containing protein Pins of Drosophila can bind to both GDP- and GTP-forms of Drosophila Galpha(o). We identify Pins GoLoco domain 1 as necessary and sufficient for this unusual interaction with Galpha(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 Galpha(o)-mediated GPCR receptor signaling, e.g., in the context of the nervous system development, where Galpha(o) acts downstream from Frizzled and redundantly with Galpha(i) to control the asymmetry of cell divisions.

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ISO 690KOPEIN, Damir, Vladimir L. KATANAEV, 2009. Drosophila GoLoco-protein Pins is a target of Galpha(o)-mediated G protein-coupled receptor signaling. In: Molecular biology of the cell. 2009, 20(17), pp. 3865-3877. ISSN 1059-1524. eISSN 1939-4586. Available under: doi: 10.1091/mbc.e09-01-0021
BibTex
@article{Kopein2009-09Droso-58033,
  year={2009},
  doi={10.1091/mbc.e09-01-0021},
  title={Drosophila GoLoco-protein Pins is a target of Galpha(o)-mediated G protein-coupled receptor signaling},
  number={17},
  volume={20},
  issn={1059-1524},
  journal={Molecular biology of the cell},
  pages={3865--3877},
  author={Kopein, Damir and Katanaev, Vladimir L.}
}
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    <dcterms:abstract xml:lang="eng">G protein-coupled receptors (GPCRs) transduce their signals through trimeric G proteins, inducing guanine nucleotide exchange on their Galpha-subunits; the resulting Galpha-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 Galpha-subunits of the Galpha(i/o) class. In most cases GoLoco binds exclusively to the GDP-loaded form of the Galpha-subunits. Here we demonstrate that the poly-GoLoco-containing protein Pins of Drosophila can bind to both GDP- and GTP-forms of Drosophila Galpha(o). We identify Pins GoLoco domain 1 as necessary and sufficient for this unusual interaction with Galpha(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 Galpha(o)-mediated GPCR receptor signaling, e.g., in the context of the nervous system development, where Galpha(o) acts downstream from Frizzled and redundantly with Galpha(i) to control the asymmetry of cell divisions.</dcterms:abstract>
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