Plasma Membrane H(+)-ATPase Regulation in the Center of Plant Physiology

Janus Falhof; Jesper Torbøl Pedersen; Anja Thoe Fuglsang; Michael Palmgren

doi:10.1016/j.molp.2015.11.002

Plasma Membrane H(+)-ATPase Regulation in the Center of Plant Physiology

Mol Plant. 2016 Mar 7;9(3):323-337. doi: 10.1016/j.molp.2015.11.002. Epub 2015 Nov 14.

Authors

Janus Falhof¹, Jesper Torbøl Pedersen¹, Anja Thoe Fuglsang¹, Michael Palmgren²

Affiliations

¹ Department of Plant and Environmental Science, Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, University of Copenhagen, 1871 Frederiksberg, Denmark.
² Department of Plant and Environmental Science, Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, University of Copenhagen, 1871 Frederiksberg, Denmark. Electronic address: palmgren@plen.ku.dk.

PMID: 26584714
DOI: 10.1016/j.molp.2015.11.002

Abstract

The plasma membrane (PM) H(+)-ATPase is an important ion pump in the plant cell membrane. By extruding protons from the cell and generating a membrane potential, this pump energizes the PM, which is a prerequisite for growth. Modification of the autoinhibitory terminal domains activates PM H(+)-ATPase activity, and on this basis it has been hypothesized that these regulatory termini are targets for physiological factors that activate or inhibit proton pumping. In this review, we focus on the posttranslational regulation of the PM H(+)-ATPase and place regulation of the pump in an evolutionary and physiological context. The emerging picture is that multiple signals regulating plant growth interfere with the posttranslational regulation of the PM H(+)-ATPase.

Keywords: blue light; hormonal regulation; pathogens; protein phosphorylation/dephosphorylation; proton pump; stomata.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Biological Transport
Cell Membrane / metabolism*
Plant Cells / metabolism*
Plant Cells / microbiology
Plant Physiological Phenomena*
Protein Processing, Post-Translational
Proton-Translocating ATPases / metabolism*

Substances

Proton-Translocating ATPases