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http://hdl.handle.net/10261/236742
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dc.contributor.author | Parra-Acero, Helena | - |
dc.contributor.author | Harcet, Matija | - |
dc.contributor.author | Sánchez-Pons, Núria | - |
dc.contributor.author | Casacuberta, Elena | - |
dc.contributor.author | Brown, Nicholas H. | - |
dc.contributor.author | Dudin, Omaya | - |
dc.contributor.author | Ruiz-Trillo, Iñaki | - |
dc.date.accessioned | 2021-04-05T13:10:02Z | - |
dc.date.available | 2021-04-05T13:10:02Z | - |
dc.date.issued | 2020-11-02 | - |
dc.identifier | doi: 10.1016/j.cub.2020.08.015 | - |
dc.identifier | e-issn: 1879-0445 | - |
dc.identifier | issn: 0960-9822 | - |
dc.identifier.citation | Current Biology 30(21): 4270-4275.e4 (2020) | - |
dc.identifier.uri | http://hdl.handle.net/10261/236742 | - |
dc.description.abstract | Parra-Acero et al. investigate cell-substrate adhesion in the filasterean C. owczarzaki, a close unicellular relative of animals. They show that cell adhesion relies on actin-dependent filopodia and is mediated by the integrin adhesome. This suggests that the role of integrins in cell-matrix adhesion was established before the emergence of animals.In animals, cell-matrix adhesions are essential for cell migration, tissue organization, and differentiation, which have central roles in embryonic development [1–6]. Integrins are the major cell surface adhesion receptors mediating cell-matrix adhesion in animals. They are heterodimeric transmembrane proteins that bind extracellular matrix (ECM) molecules on one side and connect to the actin cytoskeleton on the other [7]. Given the importance of integrin-mediated cell-matrix adhesion in development of multicellular animals, it is of interest to discover when and how this machinery arose during evolution. Comparative genomic analyses have shown that core components of the integrin adhesome pre-date the emergence of animals [8–11]; however, whether it mediates cell adhesion in non-metazoan taxa remains unknown. Here, we investigate cell-substrate adhesion in Capsaspora owczarzaki, the closest unicellular relative of animals with the most complete integrin adhesome [11, 12]. Previous work described that the life cycle of C. owczarzaki (hereafter, Capsaspora) includes three distinct life stages: adherent; cystic; and aggregative [13]. Using an adhesion assay, we show that, during the adherent life stage, C. owczarzaki adheres to surfaces using actin-dependent filopodia. We show that integrin β2 and its associated protein vinculin localize as distinct patches in the filopodia. We also demonstrate that substrate adhesion and integrin localization are enhanced by mammalian fibronectin. Finally, using a specific antibody for integrin β2, we inhibited cell adhesion to a fibronectin-coated surface. Our results suggest that adhesion to the substrate in C. owczarzaki is mediated by integrins. We thus propose that integrin-mediated adhesion pre-dates the emergence of animals. | - |
dc.description.sponsorship | This work was funded by European Research Council Consolidator Grant (ERC-2012-Co-616960) to I.R.-T.; O.D. was supported by a Swiss National Science Foundation Early PostDoc Mobility fellowship (P2LAP3_171815) and a Marie Sklodowska-Curie individual fellowship (MSCA-IF 746044). M.H. received funding from the People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme FP7/ 2007-2013/ under REA grant agreement no. 330925. N.H.B.’s work on this project was supported by a Royal Society International Exchange Grant (IE141189). The CRG/UPF Proteomics Unit is part of the of Proteored, PRB3 and is supported by grant PT17/0019 of the PE I+D+i 2013-2016, funded by ISCIII and ERDF. | - |
dc.language | eng | - |
dc.publisher | Cell Press | - |
dc.publisher | Elsevier | - |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/616960 | - |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/330925 | - |
dc.relation.isversionof | Publisher's version | - |
dc.rights | openAccess | - |
dc.title | Integrin-Mediated Adhesion in the Unicellular Holozoan Capsaspora owczarzaki | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1016/j.cub.2020.08.015 | - |
dc.relation.publisherversion | http://dx.doi.org/10.1016/j.cub.2020.08.015 | - |
dc.date.updated | 2021-04-05T13:10:02Z | - |
dc.rights.license | https://creativecommons.org/licenses/by/4.0/ | - |
dc.contributor.funder | European Research Council | - |
dc.contributor.funder | European Commission | - |
dc.contributor.funder | Swiss National Science Foundation | - |
dc.contributor.funder | Instituto de Salud Carlos III | - |
dc.relation.csic | Sí | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100000780 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100000781 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100004587 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
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