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 as pH-sensitive modulators of cell activity, for instance, via plasma membrane H+-ATPase or potassium channels.
Drabkin
A V
AV
Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, Moscow.
Trofimova
M S
MS
Smolenskaya
I N
IN
Klychnikov
O I
OI
Chelysheva
V V
VV
Babakov
A V
AV
D001692:Biological Transport; D002478:Cells, Cultured; D006027:Glycosides / Q000378:metabolism*; D006706:Homeostasis; D006863:Hydrogen-Ion Concentration; D010940:Plant Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism; D011523:Protoplasts; D011956:Receptors, Cell Surface / Q000378:metabolism*; D014675:Vegetables / Q000166:cytology / Q000378:metabolism
D006027:Glycosides; D010940:Plant Proteins; D011956:Receptors, Cell Surface; C080425:fusicoccin receptor protein, plant; C007808:fusicoccin; D006180:Proton-Translocating ATPases