Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme?

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Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme? / Gomès, Eric; Venema, Kees; Simon-Plas, Françoise; Milat, Marie Louise; Palmgren, Michael Gjedde; Blein, Jean Pierre.

In: FEBS Letters, Vol. 398, No. 1, 25.11.1996, p. 48-52.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Gomès, E, Venema, K, Simon-Plas, F, Milat, ML, Palmgren, MG & Blein, JP 1996, 'Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme?', FEBS Letters, vol. 398, no. 1, pp. 48-52. https://doi.org/10.1016/S0014-5793(96)01218-5

APA

Gomès, E., Venema, K., Simon-Plas, F., Milat, M. L., Palmgren, M. G., & Blein, J. P. (1996). Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme? FEBS Letters, 398(1), 48-52. https://doi.org/10.1016/S0014-5793(96)01218-5

Vancouver

Gomès E, Venema K, Simon-Plas F, Milat ML, Palmgren MG, Blein JP. Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme? FEBS Letters. 1996 Nov 25;398(1):48-52. https://doi.org/10.1016/S0014-5793(96)01218-5

Author

Gomès, Eric ; Venema, Kees ; Simon-Plas, Françoise ; Milat, Marie Louise ; Palmgren, Michael Gjedde ; Blein, Jean Pierre. / Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme?. In: FEBS Letters. 1996 ; Vol. 398, No. 1. pp. 48-52.

Bibtex

@article{f6f734621c0349e5b574b115d3630921,
title = "Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme?",
abstract = "The antagonistic effects of the fungal toxin beticolin-1 and of L-α-lysophosphatidylcholine (lysoPC) were investigated on the plasma membrane H+-ATPase of the plant Arabidopsis thaliana (isoform 2) expressed in yeast, using both wild-type enzyme (AHA2) and C-terminal truncated enzyme (aha2Δ92). Phosphohydrolytic activities of both enzymes were inhibited by beticolin-1, with very similar 50% inhibitory concentrations, indicating that the toxin action does not involve the C-terminal located autoinhibitory domain of the proton pump. Egg lysoPC, a compound that activates the H+-ATPase by a mechanism involving the C-terminal part of the protein, was found to be able to reverse the inhibition of AHA2 by beticolin-1. The lack of effect of other detergents and the comparison of different carbon chain length lysoPCs show that the capacity to reverse the enzyme inhibition is clearly related to their ability to activate the pump. Long chain length lysoPC was also shown to reverse the inhibition of aha2Δ92 by beticolin-1, which strongly suggests that lysoPC binds to the H+-ATPase on site(s) not located on its autoinhibitory domain.",
keywords = "Autoinhibitory domain, Beticolin, L-α-Lysophosphatidylcholine, Plasma membrane H-ATPase activation",
author = "Eric Gom{\`e}s and Kees Venema and Fran{\c c}oise Simon-Plas and Milat, {Marie Louise} and Palmgren, {Michael Gjedde} and Blein, {Jean Pierre}",
year = "1996",
month = nov,
day = "25",
doi = "10.1016/S0014-5793(96)01218-5",
language = "English",
volume = "398",
pages = "48--52",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme?

AU - Gomès, Eric

AU - Venema, Kees

AU - Simon-Plas, Françoise

AU - Milat, Marie Louise

AU - Palmgren, Michael Gjedde

AU - Blein, Jean Pierre

PY - 1996/11/25

Y1 - 1996/11/25

N2 - The antagonistic effects of the fungal toxin beticolin-1 and of L-α-lysophosphatidylcholine (lysoPC) were investigated on the plasma membrane H+-ATPase of the plant Arabidopsis thaliana (isoform 2) expressed in yeast, using both wild-type enzyme (AHA2) and C-terminal truncated enzyme (aha2Δ92). Phosphohydrolytic activities of both enzymes were inhibited by beticolin-1, with very similar 50% inhibitory concentrations, indicating that the toxin action does not involve the C-terminal located autoinhibitory domain of the proton pump. Egg lysoPC, a compound that activates the H+-ATPase by a mechanism involving the C-terminal part of the protein, was found to be able to reverse the inhibition of AHA2 by beticolin-1. The lack of effect of other detergents and the comparison of different carbon chain length lysoPCs show that the capacity to reverse the enzyme inhibition is clearly related to their ability to activate the pump. Long chain length lysoPC was also shown to reverse the inhibition of aha2Δ92 by beticolin-1, which strongly suggests that lysoPC binds to the H+-ATPase on site(s) not located on its autoinhibitory domain.

AB - The antagonistic effects of the fungal toxin beticolin-1 and of L-α-lysophosphatidylcholine (lysoPC) were investigated on the plasma membrane H+-ATPase of the plant Arabidopsis thaliana (isoform 2) expressed in yeast, using both wild-type enzyme (AHA2) and C-terminal truncated enzyme (aha2Δ92). Phosphohydrolytic activities of both enzymes were inhibited by beticolin-1, with very similar 50% inhibitory concentrations, indicating that the toxin action does not involve the C-terminal located autoinhibitory domain of the proton pump. Egg lysoPC, a compound that activates the H+-ATPase by a mechanism involving the C-terminal part of the protein, was found to be able to reverse the inhibition of AHA2 by beticolin-1. The lack of effect of other detergents and the comparison of different carbon chain length lysoPCs show that the capacity to reverse the enzyme inhibition is clearly related to their ability to activate the pump. Long chain length lysoPC was also shown to reverse the inhibition of aha2Δ92 by beticolin-1, which strongly suggests that lysoPC binds to the H+-ATPase on site(s) not located on its autoinhibitory domain.

KW - Autoinhibitory domain

KW - Beticolin

KW - L-α-Lysophosphatidylcholine

KW - Plasma membrane H-ATPase activation

UR - http://www.scopus.com/inward/record.url?scp=0030602151&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(96)01218-5

DO - 10.1016/S0014-5793(96)01218-5

M3 - Journal article

C2 - 8946951

AN - SCOPUS:0030602151

VL - 398

SP - 48

EP - 52

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -

ID: 245003467