ArticleProceedings of the National Academy of Sciences of the United States of America1997
Isoform-specific interactions of Na,K-ATPase subunits are mediated via extracellular domains and carbohydrates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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.
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.
Who cites it
16 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- β subunit affects NaBiochemistry and biophysics reports · 2022Article
- Article
- Age-related changes in Na, K-ATPase expression, subunit isoform selection and assembly in the stria vascularis lateral wall of mouse cochlea.Hearing research · 2018Article
- A possible mechanism for low affinity of silkworm NaJournal of bioenergetics and biomembranes · 2017Article
- On the Many Actions of Ouabain: Pro-Cystogenic Effects in Autosomal Dominant Polycystic Kidney Disease.Molecules (Basel, Switzerland) · 2017Review
- Homodimeric anoctamin-1, but not homodimeric anoctamin-6, is activated by calcium increases mediated by the P2Y1 and P2X7 receptors.Pflugers Archiv : European journal of physiology · 2015Article
- Characterization of SLCO5A1/OATP5A1, a solute carrier transport protein with non-classical function.PloS one · 2013Article
- Subunit isoform selectivity in assembly of Na,K-ATPase α-β heterodimers.The Journal of biological chemistry · 2012Article
- Subunit composition and role of Na+,K+-ATPases in adrenal chromaffin cells.The Journal of physiology · 2005Article
- The functional role of beta subunits in oligomeric P-type ATPases.Journal of bioenergetics and biomembranes · 2001Review
- Control of IP(3)-mediated Ca2+ puffs in Xenopus laevis oocytes by the Ca2+-binding protein parvalbumin.The Journal of physiology · 2001Article
- Surface-localized glycine transporters 1 and 2 function as monomeric proteins in Xenopus oocytes.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Na,K-ATPase subunit beta1 knock-in prevents lethality of beta2 deficiency in mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels.The EMBO journal · 1998Article
- Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene.Mammalian genome : official journal of the International Mammalian Genome Society · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional unit of the Na,K-ATPase consists of a catalytic alpha subunit noncovalently linked with a glycoprotein subunit, beta. Using ouabain binding assays and immunoprecipitation of rodent alpha/beta complexes, we show here that all six possible isozymes between three alpha and two beta isoforms can be formed in Xenopus oocytes. Two isoform-specific differences in alpha/beta interactions are observed: (i) alpha1/beta1 and alpha2/beta2 complexes, in contrast to alpha1/beta2 complexes, are stable against Triton X-100-mediated dissociation, and (ii) beta2 subunits must carry N-glycans to combine with alpha1 but not with alpha2. The interacting surfaces are mainly exposed to the extracellular side because coexpression of a truncated beta1 subunit comprising the ectodomain results in assembly with alpha1 and alpha2, but not with alpha3; the beta2 ectodomain combines with alpha2 only. A chimera consisting of 81% and 19% of the alpha1 N terminus and alpha2 C terminus, respectively, behaves like alpha2 and coprecipitates with the beta2 ectodomain. In contrast, the reciprocal chimera does not coprecipitate with the beta2 ectodomain. These results provide evidence for a selective interaction of Na,K-ATPase alpha and beta subunits.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.