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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Sprache:eng
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Zusammenfassung: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
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00172-5