Formulation of a coupled mechanism between solute diffusion, phosphatase-kinase reactions and membrane potentials for the primary active transport of phosphorylated substrates through biological membranes.
Coupled interrelations occurring between a phosphatase/kinase reaction sequence acting in unstirred layers and on both sides of a charged biomembrane pore structure are presented as a plausible kinetic model for the primary active transport of phosphorylated molecules. Simulations conducted at the cell level and with credible numerical values demonstrate that the enzymes positions strongly regulate the membrane permeability for the transported substrate. Depending on both the enzymes positions (more or less far from the membrane) and the membrane charges, the membrane may appear either impervious, either permeable or able to actively transport a phosphorylated substrate. Globally all happens as if, in function of the enzymes positions, a permanent pore may be regulated, changing from a more closed to a more open conformation.
Maïsterrena
B
B
Laboratoire de Biochimie appliquée, IUTA, University Claude Bernard-Lyon 1, 43 Boulevard du 11 Novembre 1918, 69622 Villeurbanne Cedex, France. maisterr@iuta.univ-lion1.fr
Fiaty
K
K
Charcosset
C
C
Perrin
B
B
Couturier
R
R
West
I C
IC
D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D004058:Diffusion; D007700:Kinetics; D008564:Membrane Potentials; D008954:Models, Biological; D008956:Models, Chemical; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000737:chemistry*; D021381:Protein Transport
D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases