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 |
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Format: | Artikel |
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 |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(97)00172-5 |