Skip to main page content
U.S. flag
See More

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2011 May;4(3):416-27.
doi: 10.1093/mp/ssq083. Epub 2011 Feb 7.

The role of the plasma membrane H+-ATPase in plant-microbe interactions

James Mitch Elmore  1 , Gitta Coaker
Affiliations
Review

The role of the plasma membrane H+-ATPase in plant-microbe interactions

James Mitch Elmore et al. Mol Plant. 2011 May.

Abstract

Plasma membrane (PM) H+-ATPases are the primary pumps responsible for the establishment of cellular membrane potential in plants. In addition to regulating basic aspects of plant cell function, these enzymes contribute to signaling events in response to diverse environmental stimuli. Here, we focus on the roles of the PM H+-ATPase during plant-pathogen interactions. PM H+-ATPases are dynamically regulated during plant immune responses and recent quantitative proteomics studies suggest complex spatial and temporal modulation of PM H+-ATPase activity during early pathogen recognition events. Additional data indicate that PM H+-ATPases cooperate with the plant immune signaling protein RIN4 to regulate stomatal apertures during bacterial invasion of leaf tissue. Furthermore, pathogens have evolved mechanisms to manipulate PM H+-ATPase activity during infection. Thus, these ubiquitous plant enzymes contribute to plant immune responses and are targeted by pathogens to increase plant susceptibility.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Regulation of PM H+-ATPases by Phosphorylation. ClustalW alignment of the C-terminal regulatory domain of Arabidopsis (AHA) and Nicotiana (PMA) PM H+-ATPases. Underlined residues have been identified in planta as phosphorylated. Phosphorylation status of shaded residues significantly changes during PTI responses (upper). Phosphorylation (+P) effect on enzyme activity is indicated below the alignment. Protein functional domains are indicated at the bottom. (+), increase in phosphorylation or activity. (−), decrease in phosphorylation or activity. (nd), not determined. R-I and R-II are inhibitory domains.
See this image and copyright information in PMC

References

    1. Abbas HK, Tanaka T, Duke SO, Porter JK, Wray EM, Hodges L, Sessions AE, Wang E, Merrill AH, Jr., Riley RT. Fumonisin- and AAL-toxin-induced disruption of sphingolipid metabolism with accumulation of free sphingoid bases. Plant Physiol. 1994;106:1085–1093. - PMC - PubMed
    1. Amborabé B-E, Bonmort J, Fleurat-Lessard P, Roblin G. Early events induced by chitosan on plant cells. J. Exp. Bot. 2008;59:2317–2324. - PubMed
    1. Axtell MJ, Staskawicz BJ. Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4. Cell. 2003;112:369–377. - PubMed
    1. Ayres PG. Abnormal behaviour of stomata in barley leaves infected with Rhynchosporium secalis (Oudem.) J.J.Davis. J Exp. Bot. 1972;23:683–691.
    1. Ballio A. Non-host-selective fungal phytotoxins: biochemical aspects of their mode of action. Experientia. 1991;47:783–790.

Publication types

MeSH terms

Substances