Evidence map›Paper›PMID 33688925›Full record

ReviewThe Journal of general physiology2021

FXYD proteins and sodium pump regulatory mechanisms.

John Q Yap, Jaroslava Seflova, Ryan Sweazey, Pablo Artigas, Seth L Robia

Abstract readReview
In one paragraph

Review in The Journal of general physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Trial
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  17. NaInternational journal of molecular sciences · 2024
    Review
  18. Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024
    Review
  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

5 authors.

John Q YapDepartment of Cell and Molecular Physiology, Loyola University Chicago, Maywood, IL.
Jaroslava SeflovaDepartment of Cell and Molecular Physiology, Loyola University Chicago, Maywood, IL.
Ryan SweazeyDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX.
Pablo ArtigasDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX.
Seth L RobiaDepartment of Cell and Molecular Physiology, Loyola University Chicago, Maywood, IL.

Funding

Structural Determinants of Calcium Pump RegulationR01HL092321 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI Seth L Robia · 2008 to 2026
$8.9M
New mechanisms of SERCA regulation: Dimerization and MicropeptidesR01HL143816 · NHLBI · LOYOLA UNIVERSITY CHICAGO · PI Seth L Robia, Gianluigi Veglia · 2019 to 2026
$3.6M
Production and evaluation CMT2 mouse models of ATP1A1 loss-of-function-mutation using Cre-LoxP technologyR03NS116433 · NINDS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI ARTIGAS, PABLO · 2020 to 2021
$213k
NHLBI NIH HHS R01 HL092321NHLBI NIH HHS R01 HL143816NINDS NIH HHS R03 NS116433
6 · The paper itself

Abstract

The sodium/potassium-ATPase (NKA) is the enzyme that establishes gradients of sodium and potassium across the plasma membrane. NKA activity is tightly regulated for different physiological contexts through interactions with single-span transmembrane peptides, the FXYD proteins. This diverse family of regulators has in common a domain containing a Phe-X-Tyr-Asp (FXYD) motif, two conserved glycines, and one serine residue. In humans, there are seven tissue-specific FXYD proteins that differentially modulate NKA kinetics as appropriate for each system, providing dynamic responsiveness to changing physiological conditions. Our understanding of how FXYD proteins contribute to homeostasis has benefitted from recent advances described in this review: biochemical and biophysical studies have provided insight into regulatory mechanisms, genetic models have uncovered remarkable complexity of FXYD function in integrated physiological systems, new posttranslational modifications have been identified, high-resolution structural studies have revealed new details of the regulatory interaction with NKA, and new clinical correlations have been uncovered. In this review, we address the structural determinants of diverse FXYD functions and the special roles of FXYDs in various physiological systems. We also discuss the possible roles of FXYDs in protein trafficking and regulation of non-NKA targets.

Indexed as

SodiumSodium-Potassium-Exchanging ATPaseCell MembraneHumansIon TransportPotassiumPotassiumSodiumSodium-Potassium-Exchanging ATPase

Identifiers

PMID33688925
PMCPMC7953255

What Socratic 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 Socratic graph.