ArticleThe Journal of cell biology1994
Interactions of tensin with actin and identification of its three distinct actin-binding domains.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 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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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
60 citing papers in PubMed, 171 citations in OpenAlex.
- Multi-omic responses to acute exercise in abdominal subcutaneous adipose tissue of sedentary adults: findings from MoTrPAC.bioRxiv : the preprint server for biology · 2026Article
- A novel isoform of tensin-1 promotes actin filament assembly for efficient erythroblast enucleation.Blood advances · 2025Article
- Tensins in Cancer: Integration of Their Domain Functions, Context-Dependent Regulation and Biomarker Potential.Biology · 2025Review
- The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion.PLoS genetics · 2024Article
- Hypoxia-driven TNS4 fosters HNSCC tumorigenesis by stabilizing integrin α5β1 complex and triggering FAK-mediated Akt and TGFβ signaling pathways.International journal of biological sciences · 2024Article
- LIM kinases in cardiovascular health and disease.Frontiers in physiology · 2024Review
- Cytochalasans and Their Impact on Actin Filament Remodeling.Biomolecules · 2023Review
- Tensins in Kidney Function and Diseases.Life (Basel, Switzerland) · 2023Review
- 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
- Review
- Tensin3 interaction with talin drives the formation of fibronectin-associated fibrillar adhesions.The Journal of cell biology · 2022Article
- Tensin2 Is a Novel Diagnostic Marker in GIST, Associated with Gastric Location and Non-Metastatic Tumors.Cancers · 2022Article
- Immunohistochemical Analysis of the Expression of Adhesion Proteins: TNS1, TNS2 and TNS3 in Correlation with Clinicopathological Parameters in Gastric Cancer.Biomolecules · 2021Article
- Tensins - emerging insights into their domain functions, biological roles and disease relevance.Journal of cell science · 2021Review
- Genomic Approaches Reveal Pleiotropic Effects in Crossbred Beef Cattle.Frontiers in genetics · 2021Article
- Mechano-responsiveness of fibrillar adhesions on stiffness-gradient gels.Journal of cell science · 2020Article
- Hyperactivity of Mek in TNS1 knockouts leads to potential treatments for cystic kidney diseases.Cell death & disease · 2019Article
- Article
- Identification of subcellular targeting sequences of Cten reveals its role in cell proliferation.Biochimica et biophysica acta. Molecular cell research · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Tensin, a 200-kD phosphoprotein of focal contacts, contains sequence homologies to Src (SH2 domain), and several actin-binding proteins. These features suggest that tensin may link the cell membrane to the cytoskeleton and respond directly to tyrosine kinase signalling pathways. Here we identify three distinct actin-binding domains within tensin. Recombinant tensin purified after overexpression by a baculovirus system binds to actin filaments with Kd = 0.1 microM, cross-links actin filaments at a molar ratio of 1:10 (tensin/actin), and retards actin assembly by barbed end capping with Kd = 20 nM. Tensin fragments were constructed and expressed as fusion proteins to map domains having these activities. Three regions from tensin interact with actin: two regions composed of amino acids 1 to 263 and 263 to 463, cosediment with F-actin but do not alter the kinetics of actin assembly; a region composed of amino acids 888-989, with sequence homology to insertin, retards actin polymerization. A claw-shaped tensin dimer would have six potential actin-binding sites and could embrace the ends of two actin filaments at focal contacts.
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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.