TU Darmstadt / ULB / TUbiblio

Intracellular localisation of PPI1 (proton pump interactor, isoform 1), a regulatory protein of the plasma membrane H(+)-ATPase of Arabidopsis thaliana.

Bonza, M. C. and Fusca, T. and Homann, Ulrike and Thiel, Gerhard and De Michelis, M. I. (2009):
Intracellular localisation of PPI1 (proton pump interactor, isoform 1), a regulatory protein of the plasma membrane H(+)-ATPase of Arabidopsis thaliana.
In: Plant biology (Stuttgart, Germany), pp. 869-77, 11, (6), ISSN 1435-8603, [Article]

Abstract

PPI1 (proton pump interactor isoform 1) is a novel protein able to interact with the C-terminal autoinhibitory domain of the Arabidopsis thaliana plasma membrane (PM) H(+)-ATPase. In vitro, PPI1 binds the PM H(+)-ATPase in a site different from the known 14-3-3 binding site and stimulates its activity. In this study, we analysed the intracellular localisation of PPI1. The intracellular distribution was monitored in A. thaliana cultured cells by immunolocalisation using an antiserum against the PPI1 N-terminus and in Vicia faba guard cells and epidermal cells by transient expression of a GFP::PPI1 fusion. The results indicate that the bulk of PPI1 is localised at the endoplasmic reticulum, from which it might be recruited to the PM for interaction with the H(+)-ATPase in response to as yet unidentified signals.

Item Type: Article
Erschienen: 2009
Creators: Bonza, M. C. and Fusca, T. and Homann, Ulrike and Thiel, Gerhard and De Michelis, M. I.
Title: Intracellular localisation of PPI1 (proton pump interactor, isoform 1), a regulatory protein of the plasma membrane H(+)-ATPase of Arabidopsis thaliana.
Language: English
Abstract:

PPI1 (proton pump interactor isoform 1) is a novel protein able to interact with the C-terminal autoinhibitory domain of the Arabidopsis thaliana plasma membrane (PM) H(+)-ATPase. In vitro, PPI1 binds the PM H(+)-ATPase in a site different from the known 14-3-3 binding site and stimulates its activity. In this study, we analysed the intracellular localisation of PPI1. The intracellular distribution was monitored in A. thaliana cultured cells by immunolocalisation using an antiserum against the PPI1 N-terminus and in Vicia faba guard cells and epidermal cells by transient expression of a GFP::PPI1 fusion. The results indicate that the bulk of PPI1 is localised at the endoplasmic reticulum, from which it might be recruited to the PM for interaction with the H(+)-ATPase in response to as yet unidentified signals.

Journal or Publication Title: Plant biology (Stuttgart, Germany)
Volume: 11
Number: 6
Divisions: 10 Department of Biology
?? fb10_botanik ??
10 Department of Biology > Plant Membrane Biophysics
10 Department of Biology > Plant Cell Biology
Date Deposited: 22 Jun 2011 09:13
Export:

Optionen (nur für Redakteure)

View Item View Item