Evidence map›Paper›PMID 42756595›Full record

ReviewFrontiers in cell and developmental biology2026

Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications.

Jia Tong, Liuyang Qin, Yunge Zhang, Weizhen Liu, Jie Liu, Chengbiao Lu

Abstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jia TongThe Second Affiliated Hospital of Xinxiang Medical University, Henan Key Laboratory of Biological Psychiatry (Henan Medical University), Xinxiang, Henan, China.
Liuyang QinInstitute of Psychiatry and Neuroscience, Henan Medical University, Xinxiang, Henan, China.
Yunge ZhangInstitute of Psychiatry and Neuroscience, Henan Medical University, Xinxiang, Henan, China.
Weizhen LiuInstitute of Psychiatry and Neuroscience, Henan Medical University, Xinxiang, Henan, China.
Jie LiuHenan Medical Key Laboratory for Research of Trauma and Orthopedics, The Third Affiliated Hospital of Henan Medical University, Xinxiang, Henan, China.
Chengbiao LuThe Second Affiliated Hospital of Xinxiang Medical University, Henan Key Laboratory of Biological Psychiatry (Henan Medical University), Xinxiang, Henan, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: The Na+/K+-ATPase (NKA), commonly referred to as the sodium pump, is a ubiquitous membrane protein that maintains cellular homeostasis by expelling three sodium ions from the cell and importing two potassium ions using ATP hydrolysis. This enzyme is critical for maintaining resting membrane potential, generating action potentials, and facilitating substance absorption and gland secretion. Additionally, NKA plays a significant role in overall homeostasis and has been implicated in tumor cell regulation. Aim of Review: This review aims to provide a comprehensive overview of the post-translational modifications (PTMs) that modulate the function, stability, and intracellular localization of NKA. These PTMs, including phosphorylation, glycosylation, palmitoylation, ubiquitination, and glutathionylation, have emerged as key regulators of NKA activity. By exploring these modifications, we seek to uncover novel insights into the dynamic regulation of NKA and its role in various physiological processes and disease states. Key Scientific Concept of Review: Recent research has unveiled the intricate interplay between different PTMs of NKA, highlighting their independent and synergistic effects on enzyme function. These modifications not only influence NKA's ion transport capabilities but also interact with other regulatory pathways, thereby playing a crucial role in health and disease. This review will delve into the specific types of PTMs identified on NKA subunits, their functional consequences, and the potential for these modifications to serve as therapeutic targets. By synthesizing current knowledge and identifying gaps in understanding, this review aims to advance the field and inspire future research directions.

Indexed as

crosstalkFXYDNa+/K+-ATPasepost-translational modificationsprotein function

Identifiers

PMID42756595
PMCPMC13583160

What Socratic holds

Textmetadata
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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.