Lysophosphatidylcholine specifically stimulates plasma membrane H⁺‐ATPase from corn roots

Abstract

The plasma membrane H+‐ATPase activity from corn seedling roots is shown to be stimulated 3‐ to 4‐fold by the addition of lysophosphatidylcholine (lysoPC). This effect clearly differs from that of other detergents by both the magnitude and the absence of inhibition at higher concentrations. LysoPC decreases the apparent K m for MgATP, increases V max of the ATPase reaction but does not change its pH optimum. On the contrary, the acid phosphatase activity associated with plasma membranes is not influenced by lysoPC. A lysoPC stimulation is also demonstrated for the solubilized preparation of the H+‐ATPase. It is assumed that lysoPC stimulation of the plant plasma membrane H+‐ATPase is not only due to permeabilization of the vesicles for MgATP, but also direct action on the enzyme.

Modulation of H+-ATPase Activity by Fusicoccin in Plasma Membrane Vesicles from Oat (Avena sativa L.) Roots (A Comparison of Modulation by Fusicoccin, Trypsin, and Lysophosphatidylcholine)

“…This inhibition was also observed by Pedchenko et al (1990), who used lyso-PC/protein ratios of 5 to 12.5. A distinct lyso-PC Lanfermeijer and Prin:;Plant Physiol.…”

Plant Plasma Membrane H+-ATPase in Adaptation of Plants to Abiotic Stresses

“…The activity decreased with an increase in the length of the fatty acyl chain and in the degree of unsaturation of fatty acid (Hernandez et al, 2002;Kasamo, 2003, Martz et al, 2006. Lysophosphatidylcholine (a natural detergent produced from phosphatidylcholine by phospholipase A 2 ) increased the plasma membrane H + -ATPase activity (Pedechenko et al, 1990, Regenberg et al, 1995. It was found that lysophosphatidylcholine binds to the Cterminal region of the protein and by displacing the autoinhibitory domain leads to increase of ATPase activity.…”

Endoplasmic Reticulum– and Golgi-Localized Phospholipase A2 Plays Critical Roles in Arabidopsis Pollen Development and Germination

“…In a yeast two-hybrid experiment in which we screened for interactors of PLA 2 -g and -d, we found that PLA 2 -g and -d interacted with VHA-c4, a subunit of the V-ATPase complex (see Supplemental Figure 6 online). Because PLA 2 products are known to activate V-ATPases (Palmgren and Sommarin, 1989;Pedchenko et al, 1990;Viehweger et al, 2002), the binding of these two proteins can provide a clue to the function of both PLA 2 and VHA-c4.…”