Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides.

Détails

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Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_71C8B463A843
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Mode of interaction of the Gαo subunit of heterotrimeric G proteins with the GoLoco1 motif of Drosophila Pins is determined by guanine nucleotides.
Périodique
Bioscience Reports
Auteur(s)
Lüchtenborg A.M., Purvanov V., Melnik B.S., Becker S., Katanaev V.L.
ISSN
1573-4935 (Electronic)
ISSN-L
0144-8463
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
35
Numéro
6
Pages
e00271
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: epublish
Résumé
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.
Pubmed
Web of science
Open Access
Oui
Création de la notice
19/02/2016 18:59
Dernière modification de la notice
20/08/2019 14:30
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