Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides
| Autor: | Vladimir L. Katanaev, Vladimir Purvanov, Anne-marie Lüchtenborg, Bogdan S. Melnik, Simon Becker |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Guanine
Protein subunit GTP-Binding Protein alpha Subunits Amino Acid Motifs Biophysics Cell Cycle Proteins Biology GTP-Binding Protein alpha Subunits Gi-Go urologic and male genital diseases Biochemistry chemistry.chemical_compound ddc:570 Heterotrimeric G protein Animals Drosophila Proteins Nucleotide ddc:612 Molecular Biology GoLoco Guanine Nucleotide Dissociation Inhibitors chemistry.chemical_classification nucleotide exchange Original Paper Asymmetric Cell Division heterotrimeric G proteins Cell Biology Original Papers Heterotrimeric GTP-Binding Proteins asymmetric cell division FRET GoLoco heterotrimeric G proteins nucleotide exchange Guanine Nucleotides Förster resonance energy transfer chemistry FRET Drosophila Peptides Drosophila Protein |
| Zdroj: | Bioscience Reports Bioscience Reports, vol. 35, no. 6, pp. e00271 Biosci Rep Bioscience Reports, Vol. 35, No 6 (2015) pp. e00271-e00271 |
| ISSN: | 1573-4935 0144-8463 |
| Popis: | Drosophila GoLoco-containing protein Pins atypically interacts both with GDP- and GTP-loaded forms of Gαo. We show that Pins' GoLoco1 domain ‘rotates’ on Gαo depending on its nucleotide state. This mechanism has important implications for asymmetric cell divisions. Drosophila GoLoco motif-containing protein Pins is unusual in its highly efficient interaction with both GDP- and the GTP-loaded forms of the α-subunit of the heterotrimeric Go protein. We analysed the interactions of Gαo in its two nucleotide forms with GoLoco1–the first of the three GoLoco domains of Pins–and the possible structures of the resulting complexes, through combination of conventional fluorescence and FRET measurements as well as through molecular modelling. Our data suggest that the orientation of the GoLoco1 motif on Gαo significantly differs between the two nucleotide states of the latter. In other words, a rotation of the GoLoco1 peptide in respect with Gαo must accompany the nucleotide exchange in Gαo. The sterical hindrance requiring such a rotation probably contributes to the guanine nucleotide exchange inhibitor activity of GoLoco1 and Pins as a whole. Our data have important implications for the mechanisms of Pins regulation in the process of asymmetric cell divisions. |
| Databáze: | OpenAIRE |
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