Evidence map›Paper›PMID 18420589›Full record

ArticleThe Journal of biological chemistry2008

G-protein-coupled receptor-mediated traffic of Na,K-ATPase to the plasma membrane requires the binding of adaptor protein 1 to a Tyr-255-based sequence in the alpha-subunit.

Riad Efendiev, Claudia E Budu, Alejandro M Bertorello, Carlos H Pedemonte

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. A hypomorphic mutation of the gamma-1 adaptin gene (Ap1g1) causes inner ear, retina, thyroid, and testes abnormalities in mice.Mammalian genome : official journal of the International Mammalian Genome Society · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009
    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 2 institutions in 2 countries.

Riad EfendievCollege of Pharmacy, University of Houston, Houston, Texas 77204, USA. riad.efendi@uth.tmc.edu
Claudia E Budu
Alejandro M Bertorello
Carlos H Pedemonte
University of Houston · USKarolinska University Hospital · SE

Funding

Dopamine inhibition of proximal tubule Na, K-ATPaseR01DK062195 · NIDDK · UNIVERSITY OF HOUSTON · PI PEDEMONTE, CARLOS H · 2003 to 2006
$1.0M
NIDDK NIH HHS DK62195
6 · The paper itself

Abstract

Motion of integral membrane proteins to the plasma membrane in response to G-protein-coupled receptor signals requires selective cargo recognition motifs that bind adaptor protein 1 and clathrin. Angiotensin II, through the activation of AT1 receptors, promotes the recruitment to the plasma membrane of Na,K-ATPase molecules from intracellular compartments. We present evidence to demonstrate that a tyrosine-based sequence (IVVY-255) present within the Na,K-ATPase alpha1-subunit is involved in the binding of adaptor protein 1. Mutation of Tyr-255 to a phenylalanine residue in the Na,K-ATPase alpha1-subunit greatly reduces the angiotensin II-dependent activation of Na,K-ATPase, recruitment of Na,K-ATPase molecules to the plasma membrane, and association of adaptor protein 1 with Na,K-ATPase alpha1-subunit molecules. To determine protein-protein interaction, we used fluorescence resonance energy transfer between fluorophores attached to the Na,K-ATPase alpha1-subunit and adaptor protein 1. Although angiotensin II activation of AT1 receptors induces a significant increase in the level of fluorescence resonance energy transfer between the two molecules, this effect was blunted in cells expressing the Tyr-255 mutant. Thus, results from different methods and techniques suggest that the Tyr-255-based sequence within the NKA alpha1-subunit is the site of adaptor protein 1 binding in response to the G-protein-coupled receptor signals produced by angiotensin II binding to AT1 receptors.

Indexed as

Adaptor Protein Complex 1Angiotensin IIAnimalsCell LineCell MembraneEnzyme ActivationMutationOpossumsPhenylalanineProtein BindingProtein ConformationRatsSodium-Potassium-Exchanging ATPaseTransfectionTyrosineAdaptor Protein Complex 1Angiotensin IIPhenylalanineSodium-Potassium-Exchanging ATPaseTyrosine

Identifiers

PMID18420589
PMCPMC2427321
OpenAlexW2087945501

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.