Evidence map›Paper›PMID 17078968›Full record

ArticleJournal of molecular biology2007

Janus model of the Na,K-ATPase beta-subunit transmembrane domain: distinct faces mediate alpha/beta assembly and beta-beta homo-oligomerization.

Sonali P Barwe, Sanguk Kim, Sigrid A Rajasekaran, James U Bowie, Ayyappan K Rajasekaran

Abstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Regulation of Neuronal Na,K-ATPase by Extracellular Scaffolding Proteins.International journal of molecular sciences · 2018
    Article
  6. NaJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017
    Article
  7. Article
  8. Article
  9. Ion dependence of Na-K-ATPase-mediated epithelial cell adhesion and migration.American journal of physiology. Cell physiology · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia.American journal of physiology. Cell physiology · 2012
    Review
  18. 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

5 authors.

Sonali P BarweDepartment of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California-Los Angeles, Los Angeles, CA 90095, USA.
Sanguk Kim
Sigrid A Rajasekaran
James U Bowie
Ayyappan K Rajasekaran

Funding

Membrane Protein StabilityR01GM063919 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BOWIE, JAMES U · 2001 to 2021
$5.6M
Role of Beta Subunit of Sodium Pump in Cell AdhesionR01DK056216 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI RAJASEKARAN, AYYAPPAN K. · 2001 to 2009
$2.1M
NIDDK NIH HHS DK 56216NIDDK NIH HHS R01 DK056216NIGMS NIH HHS R01 GM063919
6 · The paper itself

Abstract

Na,K-ATPase is a hetero-oligomer of alpha and beta-subunits. The Na,K-ATPase beta-subunit (Na,K-beta) is involved in both the regulation of ion transport activity, and in cell-cell adhesion. By structure prediction and evolutionary analysis, we identified two distinct faces on the Na,K-beta transmembrane domain (TMD) that could mediate protein-protein interactions: a glycine zipper motif and a conserved heptad repeat. Here, we show that the heptad repeat face is involved in the hetero-oligomeric interaction of Na,K-beta with Na,K-alpha, and the glycine zipper face is involved in the homo-oligomerization of Na,K-beta. Point mutations in the heptad repeat motif reduced Na,K-beta binding to Na,K-alpha, and Na,K-ATPase activity. Na,K-beta TMD homo-oligomerized in biological membranes, and mutation of the glycine zipper motif affected oligomerization and cell-cell adhesion. These results provide a structural basis for understanding how Na,K-beta links ion transport and cell-cell adhesion.

Indexed as

Models, MolecularProtein Structure, QuaternaryAmino Acid SequenceAnimalsCell AggregationCell MembraneDogsGlycineLeucineMolecular Sequence DataMutant ProteinsMutationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsRepetitive Sequences, Amino AcidGlycineLeucineMutant ProteinsProtein SubunitsSodium-Potassium-Exchanging ATPase

Identifiers

PMID17078968
PMCPMC2459552

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.