Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Lüchtenborg, Anne-Marie, Purvanov, Vladimir, Melnik, Bogdan S., Becker, Simon, Katanaev, Vladimir L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2015
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
_version_ 1782402832152920064
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
work_keys_str_mv AT luchtenborgannemarie modeofinteractionofthegaosubunitofheterotrimericgproteinswiththegoloco1motifofdrosophilapinsisdeterminedbyguaninenucleotides
AT purvanovvladimir modeofinteractionofthegaosubunitofheterotrimericgproteinswiththegoloco1motifofdrosophilapinsisdeterminedbyguaninenucleotides
AT melnikbogdans modeofinteractionofthegaosubunitofheterotrimericgproteinswiththegoloco1motifofdrosophilapinsisdeterminedbyguaninenucleotides
AT beckersimon modeofinteractionofthegaosubunitofheterotrimericgproteinswiththegoloco1motifofdrosophilapinsisdeterminedbyguaninenucleotides
AT katanaevvladimirl modeofinteractionofthegaosubunitofheterotrimericgproteinswiththegoloco1motifofdrosophilapinsisdeterminedbyguaninenucleotides