title: Specific Activation of the Plant P-type Plasma Membrane H+-ATPase by Lysophospholipids Depends on the Autoinhibitory N- and C-terminal Domains.
abstract: Eukaryotic P-type plasma membrane H(+)-ATPases are primary active transport systems that are regulated at the post-translation level by cis-acting autoinhibitory domains, which can be relieved by protein kinase-mediated phosphorylation or binding of specific lipid species. Here we show that lysophospholipids specifically activate a plant plasma membrane H(+)-ATPase (Arabidopsis thaliana AHA2) by a mechanism that involves both cytoplasmic terminal domains of AHA2, whereas they have no effect on the fungal counterpart (Saccharomyces cerevisiae Pma1p). The activation was dependent on the glycerol backbone of the lysophospholipid and increased with acyl chain length, whereas the headgroup had little effect on activation. Activation of the plant pump by lysophospholipids did not involve the penultimate residue, Thr-947, which is known to be phosphorylated as part of a binding site for activating 14-3-3 protein, but was critically dependent on a single autoinhibitory residue (Leu-919) upstream of the C-terminal cytoplasmic domain in AHA2. A corresponding residue is absent in the fungal counterpart. These data indicate that plant plasma membrane H(+)-ATPases evolved as specific receptors for lysophospholipids and support the hypothesis that lysophospholipids are important plant signaling molecules.
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Alex Green
authors.initials: AG
authors.lastname: Wielandt
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Jesper Torbøl
authors.initials: JT
authors.lastname: Pedersen
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Janus
authors.initials: J
authors.lastname: Falhof
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Gerdi Christine
authors.initials: GC
authors.lastname: Kemmer
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Anette
authors.initials: A
authors.lastname: Lund
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Kira
authors.initials: K
authors.lastname: Ekberg
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Anja Thoe
authors.initials: AT
authors.lastname: Fuglsang
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Thomas Günther
authors.initials: TG
authors.lastname: Pomorski
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
authors.forename: Morten Jeppe
authors.initials: MJ
authors.lastname: Buch-Pedersen
authors.affiliation: From the Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg, Denmark palmgren@plen.ku.dk.
authors.forename: Michael
authors.identifier: http://orcid.org/0000-0002-9982-6114
authors.initials: M
authors.lastname: Palmgren
mesh_terms: D017360:Arabidopsis / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000201:enzymology / Q000235:genetics; D004789:Enzyme Activation; D008246:Lysophospholipids / Q000378:metabolism*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D008246:Lysophospholipids; D029701:Saccharomyces cerevisiae Proteins; C092477:PMA1 protein, S cerevisiae; D006180:Proton-Translocating ATPases; C479903:AHA2 protein, Arabidopsis
keywords: H+-ATPase; lysophospholipid; plasma membrane; post-transcriptional regulation; proton pump