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

Mauro Marra, Vincenzo Fogliano, Alessandra Zambardi, Maria Rosaria Fullone, Daniela Nasta, Patrizia Aducci*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)293-296
Number of pages4
JournalFEBS Letters
Issue number3
Publication statusPublished - 18 Mar 1996
Externally publishedYes


  • 14-3-3 protein
  • Fusicoccin receptor
  • H-ATPase
  • Signal transduction

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