Evidence map›Paper›PMID 8458871›Full record

ArticleThe Journal of cell biology1993

Functional activation of plasma membrane anion exchangers occurs in a pre-Golgi compartment.

S Ruetz, A E Lindsey, C L Ward, R R Kopito

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Stromal uptake and transmission of acid is a pathway for venting cancer cell-generated acid.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Sensors and regulators of intracellular pH.Nature reviews. Molecular cell biology · 2010
    Review
  9. Article
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Article
  17. Article
  18. Expression of bacteriorhodopsin in Sf9 and COS-1 cells.Journal of bioenergetics and biomembranes · 1997
    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

4 authors at 1 institution in 1 country.

S RuetzDepartment of Biological Sciences, Stanford University, California 94305-5020.
A E Lindsey
C L Ward
R R Kopito
Stanford University · US

Funding

MOLECULAR AND CELLULAR BIOLOGY OF THE CFTRR01DK043994 · NIDDK · STANFORD UNIVERSITY · PI KOPITO, RON R · 1991 to 2003
$873k
NIDDK NIH HHS R01DK43994NIGMS NIH HHS R01GM8543
6 · The paper itself

Abstract

Folding and oligomerization of most plasma membrane glycoproteins, including those involved in ion transport, occur in the ER and are frequently required for their exit from this organelle. It is currently unknown, however, where or when in the biosynthetic pathway these proteins become functionally active. AE1 and AE2 are tissue-specific, plasma membrane anion transport proteins. Transient expression of AE2 in a eukaryotic cell line leads to an increase in stilbene inhibitable whole cell 35SO4(2-)-efflux consistent with its function as a plasma membrane anion exchanger. No such increased transport activity was observed in AE1 transfectants, despite the fact that the two proteins were synthesized in roughly equal portions. In contrast, both AE1 and AE2 expression resulted in significant increase in Cl-/SO4(2-)-exchange in crude microsomes demonstrating that both AE1 and AE2 cDNAs encode functional proteins. Immunofluorescence staining and pulse-chase labeling experiments revealed that while 60% of AE2 is processed to the cell surface of transfectants, AE1 is restricted to an intracellular compartment and never acquires mature oligosaccharides. Crude microsomes from transfected cells were fractionated into plasma membrane and ER-derived vesicles by con A affinity chromatography. All of the AE1 and approximately half of the cellular AE2 was eluted with the ER vesicles, confirming their intracellular localization. Anion transport measurements on these fractions confirmed that the ER-restricted anion exchangers were functional. We conclude that AE1 and AE2 acquire the ability to mediate anion exchange at an early stage of their biosynthesis, before their exit from the ER.

Indexed as

Anion Transport ProteinsAntiportersAnimalsAnionsBase SequenceCell LineCell MembraneCell Membrane PermeabilityDNAEndoplasmic ReticulumFluorescent Antibody TechniqueGolgi ApparatusHumansImmunoblottingIon TransportKidneyAnionsAnion Transport ProteinsAntiportersDNAMembrane ProteinsSLC4A ProteinsSulfates

Identifiers

PMID8458871
PMCPMC2119765
OpenAlexW2099602045

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.