ArticleThe Journal of cell biology2017
AMPK negatively regulates tensin-dependent integrin activity.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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.
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.
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Who cites it
67 citing papers in PubMed, 108 citations in OpenAlex.
- Outside-In Signaling as a Detonator-like Stimulus of Integrin Activation by Promoting Both Affinity and Avidity.Biomolecules · 2026Review
- Adhesion-derived condensates control component availability to regulate adhesion dynamics.Nature communications · 2026Article
- Talin-tensin3 interactions regulate fibrillar adhesion formation and tensin3 phase separation.The Journal of cell biology · 2026Article
- TNS1/TAGLN-enriched endometrial stromal cells is associated with a persistent fibrotic microenvironment in intrauterine adhesion.Frontiers in cell and developmental biology · 2026Article
- Cargo-selective regulation of clathrin-mediated endocytosis by AMP-activated protein kinase.iScience · 2025Article
- Tensins in Cancer: Integration of Their Domain Functions, Context-Dependent Regulation and Biomarker Potential.Biology · 2025Review
- AMP-activated protein kinase (AMPK) is essential for tendon homeostasis and prevents premature senescence and ectopic calcification.bioRxiv : the preprint server for biology · 2025Article
- Integrin and Its Associated Proteins as a Mediator for Mechano-Signal Transduction.Biomolecules · 2025Review
- Fibroblast integrin α11β1 is a collagen assembly receptor in mechanoregulated fibrillar adhesions.Matrix biology : journal of the International Society for Matrix Biology · 2024Article
- Irisin reduces senile osteoporosis by inducing osteocyte mitophagy through Ampk activation.iScience · 2024Article
- External Scaffold for Strengthening the Pulmonary Autograft in the Ross Procedure.Biomimetics (Basel, Switzerland) · 2024Review
- Tensin-2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis.Scientific reports · 2024Article
- Identification of a clinically efficacious CAR T cell subset in diffuse large B cell lymphoma by dynamic multidimensional single-cell profiling.Nature cancer · 2024Article
- Engineering metabolism to modulate immunity.Advanced drug delivery reviews · 2024Review
- Tensin-3 is involved in osteogenic versus adipogenic fate of human bone marrow stromal cells.Cellular and molecular life sciences : CMLS · 2023Article
- The βI domain promotes active β1 integrin clustering into mature adhesion sites.Life science alliance · 2023Article
- The role of tensins in malignant neoplasms.Archives of medical science : AMS · 2023Article
- TFEB controls integrin-mediated endothelial cell adhesion by the regulation of cholesterol metabolism.Angiogenesis · 2022Article
- Review
- Transient regulation of focal adhesion via Tensin3 is required for nascent oligodendrocyte differentiation.eLife · 2022Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Tight regulation of integrin activity is paramount for dynamic cellular functions such as cell matrix adhesion and mechanotransduction. Integrin activation is achieved through intracellular interactions at the integrin cytoplasmic tails and through integrin-ligand binding. In this study, we identify the metabolic sensor AMP-activated protein kinase (AMPK) as a β1-integrin inhibitor in fibroblasts. Loss of AMPK promotes β1-integrin activity, the formation of centrally located active β1-integrin- and tensin-rich mature fibrillar adhesions, and cell spreading. Moreover, in the absence of AMPK, cells generate more mechanical stress and increase fibronectin fibrillogenesis. Mechanistically, we show that AMPK negatively regulates the expression of the integrin-binding proteins tensin1 and tensin3. Transient expression of tensins increases β1-integrin activity, whereas tensin silencing reduces integrin activity in fibroblasts lacking AMPK. Accordingly, tensin silencing in AMPK-depleted fibroblasts impedes enhanced cell spreading, traction stress, and fibronectin fiber formation. Collectively, we show that the loss of AMPK up-regulates tensins, which bind β1-integrins, supporting their activity and promoting fibrillar adhesion formation and integrin-dependent processes.
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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.