Cargando…
Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy
Podosomes are highly dynamic actin-rich adhesive structures formed predominantly by cells of the monocytic lineage, which degrade the extracellular matrix. They consist of a core of F-actin and actin-regulating proteins, surrounded by a ring of adhesion-associated proteins such as vinculin. We have...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3921150/ https://www.ncbi.nlm.nih.gov/pubmed/24523880 http://dx.doi.org/10.1371/journal.pone.0088251 |
_version_ | 1782303273689022464 |
---|---|
author | Walde, Marie Monypenny, James Heintzmann, Rainer Jones, Gareth E. Cox, Susan |
author_facet | Walde, Marie Monypenny, James Heintzmann, Rainer Jones, Gareth E. Cox, Susan |
author_sort | Walde, Marie |
collection | PubMed |
description | Podosomes are highly dynamic actin-rich adhesive structures formed predominantly by cells of the monocytic lineage, which degrade the extracellular matrix. They consist of a core of F-actin and actin-regulating proteins, surrounded by a ring of adhesion-associated proteins such as vinculin. We have characterised the structure of podosomes in macrophages, particularly the structure of the ring, using three super-resolution fluorescence microscopy techniques: stimulated emission depletion microscopy, structured illumination microscopy and localisation microscopy. Rather than being round, as previously assumed, we found the vinculin ring to be created from relatively straight strands of vinculin, resulting in a distinctly polygonal shape. The strands bind preferentially at angles between 116° and 135°. Furthermore, adjacent vinculin strands are observed nucleating at the corners of the podosomes, suggesting a mechanism for podosome growth. |
format | Online Article Text |
id | pubmed-3921150 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39211502014-02-12 Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy Walde, Marie Monypenny, James Heintzmann, Rainer Jones, Gareth E. Cox, Susan PLoS One Research Article Podosomes are highly dynamic actin-rich adhesive structures formed predominantly by cells of the monocytic lineage, which degrade the extracellular matrix. They consist of a core of F-actin and actin-regulating proteins, surrounded by a ring of adhesion-associated proteins such as vinculin. We have characterised the structure of podosomes in macrophages, particularly the structure of the ring, using three super-resolution fluorescence microscopy techniques: stimulated emission depletion microscopy, structured illumination microscopy and localisation microscopy. Rather than being round, as previously assumed, we found the vinculin ring to be created from relatively straight strands of vinculin, resulting in a distinctly polygonal shape. The strands bind preferentially at angles between 116° and 135°. Furthermore, adjacent vinculin strands are observed nucleating at the corners of the podosomes, suggesting a mechanism for podosome growth. Public Library of Science 2014-02-11 /pmc/articles/PMC3921150/ /pubmed/24523880 http://dx.doi.org/10.1371/journal.pone.0088251 Text en © 2014 Walde et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Walde, Marie Monypenny, James Heintzmann, Rainer Jones, Gareth E. Cox, Susan Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy |
title | Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy |
title_full | Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy |
title_fullStr | Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy |
title_full_unstemmed | Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy |
title_short | Vinculin Binding Angle in Podosomes Revealed by High Resolution Microscopy |
title_sort | vinculin binding angle in podosomes revealed by high resolution microscopy |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3921150/ https://www.ncbi.nlm.nih.gov/pubmed/24523880 http://dx.doi.org/10.1371/journal.pone.0088251 |
work_keys_str_mv | AT waldemarie vinculinbindingangleinpodosomesrevealedbyhighresolutionmicroscopy AT monypennyjames vinculinbindingangleinpodosomesrevealedbyhighresolutionmicroscopy AT heintzmannrainer vinculinbindingangleinpodosomesrevealedbyhighresolutionmicroscopy AT jonesgarethe vinculinbindingangleinpodosomesrevealedbyhighresolutionmicroscopy AT coxsusan vinculinbindingangleinpodosomesrevealedbyhighresolutionmicroscopy |