Evidence map›Paper›PMID 33236982›Full record

ArticleeLife2020

The Arabidopsis V-ATPase is localized to the TGN/EE via a seed plant-specific motif.

Upendo Lupanga, Rachel Röhrich, Jana Askani, Stefan Hilmer, Christiane Kiefer, Melanie Krebs, Takehiko Kanazawa, Takashi Ueda, Karin Schumacher

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  12. Regulation of V-ATPase by Jasmonic Acid: Possible Role of Persulfidation.International journal of molecular sciences · 2023
    Article
  13. Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. The Plant V-ATPase.Frontiers in plant science · 2022
    Review
  19. Review
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

9 authors at 2 institutions in 2 countries.

Upendo LupangaDepartment of Cell Biology, Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.ORCID 0000-0001-7732-5012
Rachel RöhrichDepartment of Cell Biology, Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.
Jana AskaniDepartment of Cell Biology, Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.ORCID 0000-0002-1390-7344
Stefan HilmerElectron Microscopy Core Facility, Heidelberg University, Heidelberg, Germany.
Christiane KieferDepartment of Biodiversity and Plant Systematics, Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.
Melanie KrebsDepartment of Cell Biology, Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.ORCID 0000-0001-6858-3247
Takehiko KanazawaDivision of Cellular Dynamics, National Institute for Basic Biology, OkazakiAichi, Japan.
Takashi UedaDivision of Cellular Dynamics, National Institute for Basic Biology, OkazakiAichi, Japan.ORCID 0000-0002-5190-892X
Karin SchumacherDepartment of Cell Biology, Centre for Organismal Studies, Heidelberg University, Heidelberg, Germany.ORCID 0000-0001-6484-8105
Heidelberg University · DENational Institute for Basic Biology · JP

Funding

DFG SFB1101 TPA02Ministry of Education, Culture, Sports, Science and Technology 18H02470Ministry of Education, Culture, Sports, Science and Technology 18K14738Ministry of Education, Culture, Sports, Science and Technology 19H05675
6 · The paper itself

Abstract

The V-ATPase is a versatile proton-pump found in a range of endomembrane compartments yet the mechanisms governing its differential targeting remain to be determined. In Arabidopsis, VHA-a1 targets the V-ATPase to the TGN/EE whereas VHA-a2 and VHA-a3 are localized to the tonoplast. We report here that the VHA-a1 targeting domain serves as both an ER-exit and as a TGN/EE-retention motif and is conserved among seed plants. In contrast, Marchantia encodes a single VHA-isoform that localizes to the TGN/EE and the tonoplast in Arabidopsis. Analysis of CRISPR/Cas9 generated null alleles revealed that VHA-a1 has an essential function for male gametophyte development but acts redundantly with the tonoplast isoforms during vegetative growth. We propose that in the absence of VHA-a1, VHA-a3 is partially re-routed to the TGN/EE. Our findings contribute to understanding the evolutionary origin of V-ATPase targeting and provide a striking example that differential localization does not preclude functional redundancy.

Indexed as

ArabidopsisArabidopsis ProteinsCRISPR-Cas SystemsGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGenotypeMutagenesis, Site-DirectedPhylogenyPlant RootsPollenSeedsVacuolar Proton-Translocating ATPasesArabidopsis ProteinsVacuolar Proton-Translocating ATPasesVHA-a1 protein, ArabidopsisA. thalianaCRISPRMarchantia polymorphaplant biologyproton pumptargetingTGN/EEV-ATPase

Identifiers

PMID33236982
PMCPMC7717909
OpenAlexW3108818902

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.