Evidence map›Paper›PMID 21239492›Full record

ArticleThe Journal of biological chemistry2011

pH-dependent cargo sorting from the Golgi.

Chunjuan Huang, Amy Chang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Cloning and Molecular Characterization ofJournal of fungi (Basel, Switzerland) · 2022
    Article
  7. Article
  8. The role of the Golgi apparatus in disease (Review).International journal of molecular medicine · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Loss of the NaThe Journal of biological chemistry · 2017
    Article
  14. Article
  15. Article
  16. Proton Transport and pH Control in Fungi.Advances in experimental medicine and biology · 2016
    Review
  17. Article
  18. Article
  19. Article
  20. 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.

Chunjuan HuangDepartment of Molecular, Cellular & Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
Amy Chang
University of Michigan–Ann Arbor · US

Funding

TRAFFICKING PATHWAYS TO THE CELL SURFACE IN YEASTR01GM058212 · NIGMS · YESHIVA UNIVERSITY · PI CHANG, AMY Y · 1999 to 2009
$2.4M
TRAFFICKING PATHWAYS TO THE CELL SURFACE IN YEASTR55GM058212 · NIGMS · YESHIVA UNIVERSITY · PI CHANG, AMY Y · 1998 to 1998
–
NIGMS NIH HHS GM 58212NIGMS NIH HHS R01 GM058212
6 · The paper itself

Abstract

The vacuolar proton-translocating ATPase (V-ATPase) plays a major role in organelle acidification and works together with other ion transporters to maintain pH homeostasis in eukaryotic cells. We analyzed a requirement for V-ATPase activity in protein trafficking in the yeast secretory pathway. Deficiency of V-ATPase activity caused by subunit deletion or glucose deprivation results in missorting of newly synthesized plasma membrane proteins Pma1 and Can1 directly from the Golgi to the vacuole. Vacuolar mislocalization of Pma1 is dependent on Gga adaptors although no Pma1 ubiquitination was detected. Proper cell surface targeting of Pma1 was rescued in V-ATPase-deficient cells by increasing the pH of the medium, suggesting that missorting is the result of aberrant cytosolic pH. In addition to mislocalization of the plasma membrane proteins, Golgi membrane proteins Kex2 and Vrg4 are also missorted to the vacuole upon loss of V-ATPase activity. Because the missorted cargos have distinct trafficking routes, we suggest a pH dependence for multiple cargo sorting events at the Golgi.

Indexed as

Amino Acid Transport Systems, BasicBiological TransportGlucoseGolgi ApparatusHydrogen-Ion ConcentrationMembrane Transport ProteinsProprotein ConvertasesProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesAmino Acid Transport Systems, BasicCAN1 protein, S cerevisiaeGlucoseKEX2 protein, S cerevisiaeMembrane Transport ProteinsPMA1 protein, S cerevisiaeProprotein ConvertasesProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesVRG4 protein, S cerevisiae

Identifiers

PMID21239492
PMCPMC3060457
OpenAlexW2008077045

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.