Evidence map›Paper›PMID 24860096›Full record

ArticleThe Journal of biological chemistry2014

Yeast phosphofructokinase-1 subunit Pfk2p is necessary for pH homeostasis and glucose-dependent vacuolar ATPase reassembly.

Chun-Yuan Chan, Karlett J Parra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  7. Review
  8. Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  9. Review
  10. Article
  11. The Plant V-ATPase.Frontiers in plant science · 2022
    Review
  12. Review
  13. Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  14. Interaction between the yeast RAVE complex and Vph1-containing VThe Journal of biological chemistry · 2020
    Article
  15. Functional reconstitution of vacuolar HThe Journal of biological chemistry · 2019
    Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Breaking up and making up: The secret life of the vacuolar HProtein science : a publication of the Protein Society · 2017
    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

2 authors at 1 institution in 1 country.

Chun-Yuan ChanFrom the Department of Biochemistry and Molecular Biology of the School of Medicine, University of New Mexico Health Sciences Center, Albuquerque, New Mexico 87131.
Karlett J ParraFrom the Department of Biochemistry and Molecular Biology of the School of Medicine, University of New Mexico Health Sciences Center, Albuquerque, New Mexico 87131 kjparra@salud.unm.edu.
University of New Mexico · US

Funding

V-ATPase H+ PUMP REGULATION IN FUEL ENERGY SELECTIONR01GM086495 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI PARRA, KARLETT J · 2009 to 2013
$1.7M
NIGMS NIH HHS R01 GM086495NIGMS NIH HHS R01GM086495
6 · The paper itself

Abstract

V-ATPases are conserved ATP-driven proton pumps that acidify organelles. Yeast V-ATPase assembly and activity are glucose-dependent. Glucose depletion causes V-ATPase disassembly and its inactivation. Glucose readdition triggers reassembly and resumes proton transport and organelle acidification. We investigated the roles of the yeast phosphofructokinase-1 subunits Pfk1p and Pfk2p for V-ATPase function. The pfk1Δ and pfk2Δ mutants grew on glucose and assembled wild-type levels of V-ATPase pumps at the membrane. Both phosphofructokinase-1 subunits co-immunoprecipitated with V-ATPase in wild-type cells; upon deletion of one subunit, the other subunit retained binding to V-ATPase. The pfk2Δ cells exhibited a partial vma growth phenotype. In vitro ATP hydrolysis and proton transport were reduced by 35% in pfk2Δ membrane fractions; they were normal in pfk1Δ. In vivo, the pfk1Δ and pfk2Δ vacuoles were alkalinized and the cytosol acidified, suggestive of impaired V-ATPase proton transport. Overall the pH alterations were more dramatic in pfk2Δ than pfk1Δ at steady state and after readdition of glucose to glucose-deprived cells. Glucose-dependent reassembly was 50% reduced in pfk2Δ, and the vacuolar lumen was not acidified after reassembly. RAVE-assisted glucose-dependent reassembly and/or glucose signals were disturbed in pfk2Δ. Binding of disassembled V-ATPase (V1 domain) to its assembly factor RAVE (subunit Rav1p) was 5-fold enhanced, indicating that Pfk2p is necessary for V-ATPase regulation by glucose. Because Pfk1p and Pfk2p are necessary for V-ATPase proton transport at the vacuole in vivo, a role for glycolysis at regulating V-ATPase proton transport is discussed.

Indexed as

GlucoseGlycolysisIntracellular MembranesPhosphofructokinase-2Protein SubunitsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesVacuolesGlucosePhosphofructokinase-2Protein SubunitsSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesGlucosePhosphofructokinaseRAVESaccharomyces cerevisiaeV1Vo-ATPaseVacuolar AcidificationVacuolar ATPaseV-ATPaseYeast

Identifiers

PMID24860096
PMCPMC4094055
OpenAlexW1990733961

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.