ArticleThe Journal of cell biology2021
Ubiquitous membrane-bound DNase activity in podosomes and invadopodia.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- Podosomes and Mechanical Force.Results and problems in cell differentiation · 2026Review
- Myosins 1e/f at the podosome base regulate podosome dynamics and promote macrophage migration.European journal of cell biology · 2025Article
- Decoy DNA Protects Molecular Tension Probes from DNase Degradation.Angewandte Chemie (International ed. in English) · 2025Article
- High-throughput Flow-cytometry Measurement of Cellular Mechanotype Based on Rupture and Delivery of DNA Tension Probes into Cells.Journal of visualized experiments : JoVE · 2025Article
- Force-bearing phagocytic adhesion rings mediate the phagocytosis of surface-bound particles.Nature communications · 2025Article
- Origin and significance of the human DNase repertoire.Scientific reports · 2022Article
- Single-Molecule Force Imaging Reveals That Podosome Formation Requires No Extracellular Integrin-Ligand Tensions or Interactions.ACS nano · 2022Article
- Characterization of Integrin Molecular Tension of Human Breast Cancer Cells on Anisotropic Nanopatterns.Frontiers in molecular biosciences · 2022Article
- Role of Cell-Free DNA and Deoxyribonucleases in Tumor Progression.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Podosomes and invadopodia, collectively termed invadosomes, are adhesive and degradative membrane structures formed in many types of cells and are well known for recruiting various proteases. However, another major class of degradative enzymes, deoxyribonuclease (DNase), remains unconfirmed and not studied in invadosomes. Here, using surface-immobilized nuclease sensor (SNS), we demonstrated that invadosomes recruit DNase to their core regions, which degrade extracellular double-stranded DNA. We further identified the DNase as GPI-anchored membrane-bound DNase X. DNase recruitment is ubiquitous and consistent in invadosomes of all tested cell types. DNase activity exhibits within a minute after actin nucleation, functioning concomitantly with protease in podosomes but preceding it in invadopodia. We further showed that macrophages form DNase-active podosome rosettes surrounding bacteria or micropatterned antigen islets, and the podosomes directly degrade bacterial DNA on a surface, exhibiting an apparent immunological function. Overall, this work reports DNase in invadosomes for the first time, suggesting a richer arsenal of degradative enzymes in invadosomes than known before.
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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.