The formins FHOD1 and INF2 regulate inter-and intra-structural contractility of podosomes
| Autor: | Linda Panzer, Stefan Linder, Ben Joosten, Matthias Klose, Leona Trübe, Johan A. Slotman, Alessandra Cambi |
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| Přispěvatelé: | Pathology |
| Rok vydání: | 2016 |
| Předmět: |
Fetal Proteins
biology Podosome Macrophages Cancer development and immune defence Radboud Institute for Molecular Life Sciences [Radboudumc 2] Microfilament Proteins Formins Nuclear Proteins macromolecular substances Cell Biology Microfilament Protein Actins Extracellular Matrix Cell biology Contractility INF2 Podosomes biology.protein Humans Cells Cultured Actin Actin nucleation Podosome core |
| Zdroj: | Journal of Cell Science, 129(2), 298-313. Company of Biologists Ltd Europe PubMed Central Journal of Cell Science, 129, 298-313 Journal of Cell Science, 129, 2, pp. 298-313 |
| ISSN: | 0021-9533 |
| Popis: | Item does not contain fulltext Podosomes are actin-rich adhesion structures that depend on Arp2/3-complex-based actin nucleation. We now report the identification of the formins FHOD1 and INF2 as novel components and additional actin-based regulators of podosomes in primary human macrophages. FHOD1 surrounds the podosome core and is also present at podosome-connecting cables, whereas INF2 localizes at the podosome cap structure. Using a variety of microscopy-based methods; including a semiautomated podosome reformation assay, measurement of podosome oscillations, FRAP analysis of single podosomes, and structured illumination microscopy, both formins were found to regulate different aspects of podosome-associated contractility, with FHOD1 mediating actomyosin contractility between podosomes, and INF2 regulating contractile events at individual podosomes. Moreover, INF2 was found to be a crucial regulator of podosome de novo formation and size. Collectively, we identify FHOD1 and INF2 as novel regulators of inter- and intra-structural contractility of podosomes. Podosomes thus present as one of the few currently identified structures which depend on the concerted activity of both Arp2/3 complex and specific formins and might serve as a model system for the analysis of complex actin architectures in cells. |
| Databáze: | OpenAIRE |
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