Evidence map›Paper›PMID 10684257›Full record

ArticleThe Journal of cell biology2000

A transmembrane segment determines the steady-state localization of an ion-transporting adenosine triphosphatase.

L A Dunbar, P Aronson, M J Caplan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. 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
3.3field-weighted citation impact, top 7% 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, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. The Apical Localization of NaFrontiers in physiology · 2016
    Article
  4. Article
  5. Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014
    Review
  6. Pancreatic bicarbonate secretion involves two proton pumps.The Journal of biological chemistry · 2011
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Sodium pump localization in epithelia.Journal of bioenergetics and biomembranes · 2007
    Review
  13. Article
  14. MAL decreases the internalization of the aquaporin-2 water channel.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  15. Splice-site A choice targets plasma-membrane Ca2+-ATPase isoform 2 to hair bundles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006
    Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

L A DunbarDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510, USA. ldunbar@biomed.med.yale.edu
P Aronson
M J Caplan
Yale University · US

Funding

ION PUMPS IN POLARIZED EPITHELIA: SORTING AND FUNCTIONR01GM042136 · NIGMS · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 1989 to 2004
$1.7M
NIGMS NIH HHS GM42136NIGMS NIH HHS R01 GM042136
6 · The paper itself

Abstract

The H,K-adenosine triphosphatase (ATPase) of gastric parietal cells is targeted to a regulated membrane compartment that fuses with the apical plasma membrane in response to secretagogue stimulation. Previous work has demonstrated that the alpha subunit of the H, K-ATPase encodes localization information responsible for this pump's apical distribution, whereas the beta subunit carries the signal responsible for the cessation of acid secretion through the retrieval of the pump from the surface to the regulated intracellular compartment. By analyzing the sorting behaviors of a number of chimeric pumps composed of complementary portions of the H, K-ATPase alpha subunit and the highly homologous Na,K-ATPase alpha subunit, we have identified a portion of the gastric H,K-ATPase, which is sufficient to redirect the normally basolateral Na,K-ATPase to the apical surface in transfected epithelial cells. This motif resides within the fourth of the H,K-ATPase alpha subunit's ten predicted transmembrane domains. Although interactions with glycosphingolipid-rich membrane domains have been proposed to play an important role in the targeting of several apical membrane proteins, the apically located chimeras are not found in detergent-insoluble complexes, which are typically enriched in glycosphingolipids. Furthermore, a chimera incorporating the Na, K-ATPase alpha subunit fourth transmembrane domain is apically targeted when both of its flanking sequences derive from H,K-ATPase sequence. These results provide the identification of a defined apical localization signal in a polytopic membrane transport protein, and suggest that this signal functions through conformational interactions between the fourth transmembrane spanning segment and its surrounding sequence domains.

Indexed as

Cell PolarityAmino Acid SequenceAnimalsBiological TransportCationsCell LineCell MembraneGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationMembrane ProteinsMolecular Sequence DataOuabainParietal Cells, GastricProtein Sorting SignalsCationsGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseMembrane ProteinsOuabainProtein Sorting SignalsRecombinant Fusion ProteinsSodium-Potassium-Exchanging ATPase

Identifiers

PMID10684257
PMCPMC2169368
OpenAlexW2148190721

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.