Non-selective cation channel activity of aquaporin AtPIP2;1 regulated by Ca2+and pH.
The aquaporin AtPIP2;1 is an abundant plasma membrane intrinsic protein in Arabidopsis thaliana that is implicated in stomatal closure, and is highly expressed in plasma membranes of root epidermal cells. When expressed in Xenopus laevis oocytes, AtPIP2;1 increased water permeability and induced a non-selective cation conductance mainly associated with Na+. A mutation in the water pore, G103W, prevented both the ionic conductance and water permeability of PIP2;1. Co-expression of AtPIP2;1 with AtPIP1;2 increased water permeability but abolished the ionic conductance. AtPIP2;2 (93% identical to AtPIP2;1) similarly increased water permeability but not ionic conductance. The ionic conductance was inhibited by the application of extracellular Ca2+and Cd2+, with Ca2+giving a biphasic dose-response with a prominent IC50of 0.32 mм comparable with a previous report of Ca2+sensitivity of a non-selective cation channel (NSCC) in Arabidopsis root protoplasts. Low external pH also inhibited ionic conductance (IC50pH 6.8). Xenopus oocytes and Saccharomyces cerevisiae expressing AtPIP2;1 accumulated more Na+than controls. Establishing whether AtPIP2;1 has dual ion and water permeability in planta will be important in understanding the roles of this aquaporin and if AtPIP2;1 is a candidate for a previously reported NSCC responsible for Ca2+and pH sensitive Na+entry into roots.
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Caitlin S
CS
Byrt
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Manchun
M
Zhao
Discipline of Physiology, School of Medicine, University of Adelaide, South Australia, 5005, Australia.
Mohamad
M
Kourghi
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Jayakumar
J
Bose
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Sam W
SW
Henderson
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Jiaen
J
Qiu
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Matthew
M
Gilliham
Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Carolyn
C
Schultz
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Manuel
M
Schwarz
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Sunita A
SA
Ramesh
Discipline of Physiology, School of Medicine, University of Adelaide, South Australia, 5005, Australia.
Andrea
A
Yool
Australian Research Council Centre of Excellence in Plant Energy Biology, Waite Research Institute and School of Agriculture, Food and Wine, The University of Adelaide, Glen Osmond, South Australia, 5064, Australia.
Steve
S
Tyerman
D019943:Amino Acid Substitution; D000818:Animals; D020346:Aquaporins / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002104:Cadmium / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism* / Q000494:pharmacology; D018506:Gene Expression Regulation, Plant; D005998:Glycine / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D009865:Oocytes / Q000187:drug effects / Q000502:physiology; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics; D012964:Sodium / Q000378:metabolism; D014364:Tryptophan / Q000235:genetics; D014867:Water / Q000378:metabolism; D014982:Xenopus laevis; D008565:Membrane Proteins
D020346:Aquaporins; D029681:Arabidopsis Proteins; D002104:Cadmium; D002118:Calcium; D005998:Glycine; D011994:Recombinant Proteins; D012964:Sodium; D014364:Tryptophan; D014867:Water; C491680:plasma membrane intrinsic protein 2 Arabidopsis; C085550:At2g45960 protein, Arabidopsis; D008565:Membrane Proteins
PIP; ion transport; plasma membrane; root; water transport