Evidence map›Paper›PMID 25971968›Full record

ArticleThe Journal of biological chemistry2015

Specific Activation of the Plant P-type Plasma Membrane H+-ATPase by Lysophospholipids Depends on the Autoinhibitory N- and C-terminal Domains.

Alex Green Wielandt, Jesper Torbøl Pedersen, Janus Falhof, Gerdi Christine Kemmer, Anette Lund, Kira Ekberg, Anja Thoe Fuglsang, Thomas Günther Pomorski, Morten Jeppe Buch-Pedersen, Michael Palmgren

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. ACS omega · 2023
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  4. Article
  5. Review
  6. Article
  7. Article
  8. MPK6 Kinase Regulates Plasma Membrane HInternational journal of molecular sciences · 2021
    Article
  9. Link between Lipid Second Messengers and Osmotic Stress in Plants.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Plasma membrane HNature communications · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Alex Green WielandtFrom 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.
Jesper Torbøl PedersenFrom 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.
Janus FalhofFrom 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.
Gerdi Christine KemmerFrom 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.
Anette LundFrom 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.
Kira EkbergFrom 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.
Anja Thoe FuglsangFrom 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.
Thomas Günther PomorskiFrom 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.
Morten Jeppe Buch-PedersenFrom 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.
Michael PalmgrenFrom 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.ORCID http://orcid.org/0000-0002-9982-6114
Danish National Research Foundation · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneEnzyme ActivationLysophospholipidsPhosphorylationProtein Structure, TertiaryProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAHA2 protein, ArabidopsisArabidopsis ProteinsLysophospholipidsPMA1 protein, S cerevisiaeProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsH+-ATPaselysophospholipidplasma membranepost-transcriptional regulationproton pump

Identifiers

PMID25971968
PMCPMC4481227
OpenAlexW2218378168

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.