Evidence map›Paper›PMID 25271159›Full record

ArticleThe Journal of biological chemistry2014

Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p.

Anne M Smardon, Patricia M Kane

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Article
  10. The Role of Secretory Pathways inJournal of fungi (Basel, Switzerland) · 2020
    Review
  11. Article
  12. AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019
    Review
  13. Frontiers in microbiology · 2019
    Article
  14. Article
  15. Review
  16. Sodium Acetate Responses inFrontiers in microbiology · 2018
    Review
  17. Article
  18. Article
  19. Proton Transport and pH Control in Fungi.Advances in experimental medicine and biology · 2016
    Review
  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

2 authors at 1 institution in 1 country.

Anne M SmardonDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, New York 13210.
Patricia M KaneDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, New York 13210. Electronic address: kanepm@upstate.edu.
SUNY Upstate Medical University · US

Funding

SUBUNIT STRUCTURE/FUNCTION IN VACUOLAR H+ ATPASESR01GM050322 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI KANE, PATRICIA M · 1994 to 2015
$4.1M
NIGMS NIH HHS R01 GM050322NIGMS NIH HHS R01 GM50322
6 · The paper itself

Abstract

Yeast mutants lacking the intracellular V-ATPase proton pump (vma mutants) have reduced levels of the Pma1p proton pump at the plasma membrane and increased levels in organelles including the vacuolar lumen. We examined the mechanism and physiological consequences of Pma1p mislocalization. Pma1p is ubiquitinated in vma mutants, and ubiquitination depends on the ubiquitin ligase Rsp5p and the arrestin-related adaptor protein Rim8p. vma mutant strains containing rsp5 or rim8 mutations maintain Pma1p at the plasma membrane, suggesting that ubiquitination is required for Pma1p internalization. Acute inhibition of V-ATPase activity with concanamycin A triggers Pma1p ubiquitination and internalization. In an endocytosis-deficient mutant (end4Δ) Pma1p is ubiquitinated but retained at the plasma membrane during concanamycin A treatment. Consistent with specificity in signaling loss of V-ATPase activity to Pma1p, another plasma membrane transporter, Mup1p, is not internalized in a vma mutant, and loss of the Mup1p adaptor Art1p does not prevent Pma1p internalization in a vma mutant. Very poor growth of vma2 rsp5-1 and vma2 rim8Δ double mutants suggests that Pma1p internalization benefits the vma mutants. We hypothesize that loss of V-ATPase-mediated organelle acidification signals ubiquitination, internalization, and degradation of a portion of Pma1p as a means of balancing overall pH homeostasis.

Indexed as

Cell Cycle ProteinsCell MembraneEndocytosisEndosomal Sorting Complexes Required for TransportHydrogen-Ion ConcentrationIntracellular Signaling Peptides and ProteinsIon TransportMacrolidesMicroscopy, FluorescenceMutationOligonucleotidesProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesCell Cycle Proteinsconcanamycin AEndosomal Sorting Complexes Required for TransportIntracellular Signaling Peptides and ProteinsMacrolidesOligonucleotidesPMA1 protein, S cerevisiaeProton-Translocating ATPasesRim8 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesVacuolar Proton-Translocating ATPasesArrestinEndocytosispH RegulationPlasma Membrane Proton PumpsUbiquitinationVacuolar AcidificationVacuolar ATPaseYeast

Identifiers

PMID25271159
PMCPMC4231704
OpenAlexW2071543496

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.