ArticleCell cycle (Georgetown, Tex.)2011
Nuclear import of a lipid-modified transcription factor: mobilization of NFAT5 isoform a by osmotic stress.
Article in Cell cycle (Georgetown, Tex.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- NFAT5: a stress-related transcription factor with multiple functions in health and disease.Cell stress · 2025Review
- The membrane-associated β2e-subunit of voltage-gated calcium channels translocates to the nucleus and regulates gene expression.Frontiers in physiology · 2025Article
- NFAT5 Restricts Bovine Herpesvirus 1 Productive Infection in MDBK Cell Cultures.Microbiology spectrum · 2023Article
- S-acylated and nucleus-localized SALT OVERLY SENSITIVE3/CALCINEURIN B-LIKE4 stabilizes GIGANTEA to regulate Arabidopsis flowering time under salt stress.The Plant cell · 2023Article
- Transcription factor dynamics in plants: Insights and technologies for in vivo imaging.Plant physiology · 2022Review
- Proteolytic Activation of Plant Membrane-Bound Transcription Factors.Frontiers in plant science · 2022Review
- Review
- NFAT5 Controls the Integrity of Epidermis.Frontiers in immunology · 2021Article
- Actin Beta-Like 2 as a New Mediator of Proliferation and Migration in Epithelial Ovarian Cancer.Frontiers in oncology · 2021Article
- Role of NFAT5 in the Immune System and Pathogenesis of Autoimmune Diseases.Frontiers in immunology · 2019Review
- Nutrient-Dependent Changes of Protein Palmitoylation: Impact on Nuclear Enzymes and Regulation of Gene Expression.International journal of molecular sciences · 2018Review
- The nuclear transportation routes of membrane-bound transcription factors.Cell communication and signaling : CCS · 2018Review
- NFAT5 Isoform C Controls Biomechanical Stress Responses of Vascular Smooth Muscle Cells.Frontiers in physiology · 2018Article
- Localization and Expression of Nuclear Factor of Activated T-Cells 5 in Myoblasts Exposed to Pro-inflammatory Cytokines or Hyperosmolar Stress and in Biopsies from Myositis Patients.Frontiers in physiology · 2018Article
- A Lipid-Anchored NAC Transcription Factor Is Translocated into the Nucleus and ActivatesThe Plant cell · 2017Article
- Peptide affinity analysis of proteins that bind to an unstructured NH2-terminal region of the osmoprotective transcription factor NFAT5.Physiological genomics · 2016Article
- Article
- Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.Proteomics · 2015Article
- The physiology of protein S-acylation.Physiological reviews · 2015Review
- NFAT as cancer target: mission possible?Biochimica et biophysica acta · 2014Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipid-modified transcription factors (TFs) are biomolecular oddities since their reduced mobility and membrane attachment appear to contradict nuclear import required for their gene-regulatory function. NFAT5 isoform a (selected from an in silico screen for predicted lipid-modified TFs) is shown to contribute about half of all endogenous expression of human NFAT5 isoforms in the isotonic state. Wild-type NFAT5a protein is indeed myristoylated and palmitoylated on its transport to the plasmalemma via the endoplasmic reticulum and the Golgi. In contrast, its lipid anchor-deficient mutants as well as isoforms NFAT5b/c are diffusely localized in the cytoplasm without preference to vesicular structures. Quantitative/live microscopy shows the plasmamembrane-bound fraction of NFAT5a moving into the nucleus upon osmotic stress despite the lipid anchoring. The mobilization mechanism is not based on proteolytic processing of the lipid-anchored N-terminus but appears to involve reversible palmitoylation. Thus, NFAT5a is an example of TFs immobilized with lipid anchors at cyotoplasmic membranes in the resting state and that, nevertheless, can translocate into the nucleus upon signal induction.
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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.