Plant cell pH-static circuit mediated by fusicoccin-binding proteins

On sugar beet protoplasts that carry two types of fusicoccin-binding sites, a pH downshift in a physiological range (7.0–6.6) markedly enhanced the efficiency of fusicoccin (FC) binding, mainly owing to increased avidity of low-affinity FC-binding sites. This may allow the FC-binding proteins to act...

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Veröffentlicht in:FEBS letters 1997-03, Vol.405 (2), p.145-147
Hauptverfasser: Drabkin, Artem V, Trofimova, Marina S, Smolenskaya, Irina N, Klychnikov, Oleg I, Chelysheva, Vera V, Babakov, Alexey V
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container_issue 2
container_start_page 145
container_title FEBS letters
container_volume 405
creator Drabkin, Artem V
Trofimova, Marina S
Smolenskaya, Irina N
Klychnikov, Oleg I
Chelysheva, Vera V
Babakov, Alexey V
description On sugar beet protoplasts that carry two types of fusicoccin-binding sites, a pH downshift in a physiological range (7.0–6.6) markedly enhanced the efficiency of fusicoccin (FC) binding, mainly owing to increased avidity of low-affinity FC-binding sites. This may allow the FC-binding proteins to act as pH-sensitive modulators of cell activity, for instance, via plasma membrane H+-ATPase or potassium channels. © 1997 Federation of European Biochemical Societies
doi_str_mv 10.1016/S0014-5793(97)00172-5
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subjects Affinity
Biological Transport
Cells, Cultured
Cytoplasmic pH
Fusicoccin
Fusicoccin-binding protein
Glycosides - metabolism
Homeostasis
Hydrogen-Ion Concentration
Plant Proteins - metabolism
Proton-Translocating ATPases - metabolism
Protoplast
Protoplasts
Receptors, Cell Surface - metabolism
Vegetables - cytology
Vegetables - metabolism
title Plant cell pH-static circuit mediated by fusicoccin-binding proteins
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