Evidence map›Paper›PMID 21189264›Full record

ArticleThe Journal of biological chemistry2011

Identification of a potential receptor that couples ion transport to protein kinase activity.

Qiqi Ye, Zhichuan Li, Jiang Tian, Jeffrey X Xie, Lijun Liu, Zijian Xie

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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. A Human-Specific De Novo Gene Promotes Cortical Expansion and Folding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Na⁺Molecules (Basel, Switzerland) · 2017
    Review
  10. Article
  11. Src-independent ERK signaling through the rat α3 isoform of Na/K-ATPase.American journal of physiology. Cell physiology · 2017
    Article
  12. Review
  13. Do Src Kinase and Caveolin Interact Directly with Na,K-ATPase?The Journal of biological chemistry · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

6 authors at 1 institution in 1 country.

Qiqi YeDepartment of Physiology, University of Toledo College of Medicine, Toledo, Ohio 43614, USA.
Zhichuan Li
Jiang Tian
Jeffrey X Xie
Lijun Liu
Zijian Xie
University of Toledo · US

Funding

STRUCTURE/FUNCTION RELATIONSHIPS OF OUBAIN SENSITIVE ION PUMPSP01HL036573 · NHLBI · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI GARLID, KEITH D · 1986 to 2013
$16.4M
Na,K-ATPase as an Integrator of the Calcium-signaling MachineryR01GM078565 · NIGMS · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI XIE, ZIJIAN · 2007 to 2010
$1.2M
NHLBI NIH HHS HL-36573NHLBI NIH HHS P01 HL036573NIGMS NIH HHS GM-78565NIGMS NIH HHS R01 GM078565
6 · The paper itself

Abstract

In our previous studies, we have demonstrated that the Src-coupled α1 Na/K-ATPase works as a receptor for cardiotonic steroids, such as ouabain, to regulate cellular protein kinase cascades. Here, we explore further the structural determinants of the interaction between the α1 Na/K-ATPase and Src and demonstrate that the Src-coupled α1 Na/K-ATPase allows the cell to decode the transmembrane transport activity of the Na/K-ATPase to turn on/off protein kinases. The α1 Na/K-ATPase undergoes E1/E2 conformational transition during an ion pumping cycle. The amount of E1 and E2 Na/K-ATPase is regulated by extracellular K(+) and intracellular Na(+). Using purified enzyme preparations we find that the E1 Na/K-ATPase can bind both the Src SH2 and kinase domains simultaneously and keep Src in an inactive state. Conversely, the E1 to E2 transition releases the kinase domain and activates the associated Src. Moreover, we demonstrate that changes in E1/E2 Na/K-ATPase by either Na(+) or K(+) are capable of regulating Src and Src effectors in live cells. Together, the data suggest that the Src-coupled α1 Na/K-ATPase may act as a Na(+)/K(+) receptor, allowing salt to regulate cellular function through Src and Src effectors.

Indexed as

Cell LineEnzyme ActivationHumansIon TransportPotassiumProtein Structure, TertiarySodiumSodium-Potassium-Exchanging ATPasesrc-Family KinasesPotassiumSodiumSodium-Potassium-Exchanging ATPasesrc-Family Kinases

Identifiers

PMID21189264
PMCPMC3057788
OpenAlexW2021428453

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.