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Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides
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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660580/ https://www.ncbi.nlm.nih.gov/pubmed/26487707 http://dx.doi.org/10.1042/BSR20150201 |
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author | Lüchtenborg, Anne-Marie Purvanov, Vladimir Melnik, Bogdan S. Becker, Simon Katanaev, Vladimir L. |
author_facet | Lüchtenborg, Anne-Marie Purvanov, Vladimir Melnik, Bogdan S. Becker, Simon Katanaev, Vladimir L. |
author_sort | Lüchtenborg, Anne-Marie |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4660580 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-46605802015-12-09 Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides Lüchtenborg, Anne-Marie Purvanov, Vladimir Melnik, Bogdan S. Becker, Simon Katanaev, Vladimir L. Biosci Rep Original Papers 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. Portland Press Ltd. 2015-11-26 /pmc/articles/PMC4660580/ /pubmed/26487707 http://dx.doi.org/10.1042/BSR20150201 Text en © 2015 Authors http://creativecommons.org/licenses/by/3.0/ This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution Licence 3.0 (http://creativecommons.org/licenses/by/3.0/) . |
spellingShingle | Original Papers Lüchtenborg, Anne-Marie Purvanov, Vladimir Melnik, Bogdan S. Becker, Simon Katanaev, Vladimir L. Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides |
title | Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides |
title_full | Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides |
title_fullStr | Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides |
title_full_unstemmed | Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides |
title_short | Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides |
title_sort | mode of interaction of the gαo subunit of heterotrimeric g proteins with the goloco1 motif of drosophila pins is determined by guanine nucleotides |
topic | Original Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4660580/ https://www.ncbi.nlm.nih.gov/pubmed/26487707 http://dx.doi.org/10.1042/BSR20150201 |
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