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)

Lanfermeijer, Frank C.; Prins, H. B. A.

doi:10.1104/pp.104.4.1277

Cited by 72 publications

(53 citation statements)

References 33 publications

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“…The activated form of AHA2 was characterized by having increased V max at pH values between 6.8 and 7.5. This kinetic behaviour of the activated AHA2 resembles that of H ϩ -ATPase activated by fusicoccin in planta (Johansson et al, 1993;Lanfermeijer and Prins, 1994;Rasi-Caldogno et al, 1993). Removal of the C-terminal regulatory domain by genetic means results in a similar shift of the pH profile (Regenberg et al, 1995).…”

Section: -3-3 Proteins Activate Plant H ϩ -Atpase Provided Fusicoccmentioning

confidence: 67%

Summary

Baunsgaard¹,

Fuglsang²,

Jahn³

et al. 1998

The Plant Journal

202

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SummaryThe plasma membrane H ϩ -ATPase in higher plants has been implicated in nutrient uptake, phloem loading, elongation growth and establishment of turgor. Although a C-terminal regulatory domain has been identified, little is known about the physiological factors involved in controlling the activity of the enzyme. To identify components which play a role in the regulation of the plant H ϩ -ATPase, a fusicoccin responsive yeast expressing Arabidopsis plasma membrane H ϩ -ATPase AHA2 was employed. By testing the fusicoccin binding activity of yeast membranes, the C-terminal regulatory domain of AHA2 was found to be part of a functional fusicoccin receptor, a component of which was the 14-3-3 protein. ATP hydrolytic activity of AHA2 expressed in yeast internal membranes was activated by all tested isoforms of the 14-3-3 protein of yeast and Arabidopsis, but only in the presence of fusicoccin, and activation was prevented by a phosphoserine peptide representing a known 14-3-3 protein binding motif in Raf-1. The results demonstrate that the 14-3-3 protein is an activator molecule of the H ϩ -ATPase and provides the first evidence of a protein involved in activation of plant plasma membrane H ϩ -ATPase.

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Section: -3-3 Proteins Activate Plant H ϩ -Atpase Provided Fusicoccmentioning

confidence: 67%

Summary

Baunsgaard¹,

Fuglsang²,

Jahn³

et al. 1998

The Plant Journal

202

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“…The fungal phytotoxin fusicoccin (FC) 1 activates the plant plasma membrane H ϩ -ATPase by a process involving the Cterminal domain of the pump (6,7). To date it is well established that FC binds to and subsequently stabilizes a complex consisting of the enzyme's C terminus and 14-3-3 proteins (8 -10).…”

mentioning

confidence: 99%

Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region

Jelich-Ottmann

Weiler

Oecking

2001

Journal of Biological Chemistry

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The plant plasma membrane H؉ -ATPase is activated by the binding of 14-3-3 proteins to its extreme C-terminal amino acids (YTV) and phosphorylation of the penultimate threonine (YpTV) is necessary for this interaction in vivo. However, in the presence of the fungal toxin fusicoccin (FC), binding of 14-3-3 proteins occurs independently of phosphorylation but still involves the YTV motif. Since FC exclusively binds to the complex consisting of both 14-3-3 homologs and the C-terminal domain of the H ؉ -ATPase, the toxin was used as a tool to reveal potential protein-protein interaction sites in the enzyme's C terminus. We performed in vitro interaction studies by applying various C-terminal parts of the H ؉ -ATPase PMA2 from Nicotiana plumbaginifolia expressed as glutathione S-transferase fusion peptides in E. coli. Interestingly, the PMA2 region encompassing residues 905-922 is implicated in FC-dependent binding of 14-3-3 homologs. Recently, part of this region has been shown to contribute to the autoinhibitory action of the PMA2 C terminus. Site-directed mutagenesis of individual amino acids localized within this region resulted in a drastic decrease in FC-dependent binding of 14-3-3 proteins. Furthermore, by expressing the corresponding mutants of PMA2 in yeast, we observed a reduced capability of the mutant enzymes to functionally replace the endogenous H ؉ -ATPase. Notably, the decreased activity of the mutant enzymes was accompanied by a weakened binding of yeast 14-3-3 homologs to the plasma membrane of transformed cells. Taken together, our results suggest that a section of the autoinhibitory C-terminal PMA2 region contributes to binding of activatory 14-3-3 proteins in the absence of FC.

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“…As expected, membranes from FC-treated roots showed a stimulation of the vanadate-sensitive, ATP-hydrolysing activity tested at pH 7.4. The stimulation over the control ranged from 50 to 100%, depending on the preparation and the ratio of the ATP-hydrolytic activity between pH 6.5 and 7.4 was 2 for the control and 1 for the FC-activated enzyme [10][11][12]. Interestingly, it was found that during two-phase partitioning the in vivo-bound FC was released (data not shown), so that purified membranes from FC-treated roots were still able to bind [aH]FC.…”

Section: Resultsmentioning

confidence: 99%

“…Since it has been demonstrated that the trypsin-activated H÷-ATPase shows biochemical features very similar to those induced by FC activation [10][11][12], the same purification procedure was also used to solubilise and purify the membranebound, trypsin-activated H+-ATPase. The ratio of its ATPhydrolytic activity at pH 6.5 and 7.4 was compared to that of the H+-ATPase purified from control membranes.…”

Section: Resultsmentioning

confidence: 99%

“…It has been established that activation of the H+-ATPase is more remarkable when FC is administered in vivo to plant tissues and that it is maintained after plasma membrane isolation [9]. The biochemical features of the membrane-bound, FC-activated H+-ATPase have been determined and, on the basis of its striking similarity to trypsin activation, it has been concluded that FC stimulation is mediated by the displacement of the Cterminal autoinhibitory domain of the enzyme [10][11][12]. The molecular mechanism which leads to the FC-induced C-terminus displacement is nevertheless still undetermined and at least two different models have been proposed.…”

Section: Introductionmentioning

confidence: 99%

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The H⁺‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

et al. 1996

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The activity of 'P-type' ATPases is modulated through the C-terminal autoinhibitory domain. The molecular bases of this regulation are unknown. Their understanding demands functional and structural studies on the activated purified enzyme. In this paper the plasma membrane H+-ATPase from maize roots activated in vivo by fusicoccin was solubilised and fractionated by anion-exchange HPLC. Results showed that the H+-ATPase separated from fusicoccin receptors retained fusicoccin activation and that it was more evident after enzyme insertion into liposomes. These data suggest that fusicoccin stimulation does not depend on a direct action of the fusicoccin receptor on the H+-ATPase, but rather, fusicoccin brings about a permanent modification of the H+-ATPase which very likely represents a general regulatory mechanism for 'P-type' ATPases.

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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)

Cited by 72 publications

References 33 publications

Summary

Summary

Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region

The H⁺‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

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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)

Cited by 72 publications

References 33 publications

Summary

Summary

Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region

The H+‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

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The H⁺‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation