Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/94130
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | A Common Clathrin-Mediated Machinery Co-ordinates Cell–Cell Adhesion and Bacterial Internalization |
Autor: | Bonazzi, Matteo; Kühbacher, Andreas; Toledo-Arana, Alejandro CSIC ORCID ; Mallet, Adeline; Vasudevan, Shrihari; Pizarro-Cerdá, Javier; Brodsky, Frances M.; Cossart, Pascale | Palabras clave: | Listeria monocytogenes Actin Adherens junctions E-cadherin Internalin |
Fecha de publicación: | dic-2012 | Editor: | Wiley-Blackwell | Citación: | Traffic 13(12): 1653–1666 (2012) | Resumen: | Invasive bacterial pathogens often target cellular proteins involved in adhesion as a first event during infection. For example, Listeria monocytogenes uses the bacterial protein InlA to interact with E-cadherin, hijack the host adherens junction (AJ) machinery and invade non-phagocytic cells by a clathrin-dependent mechanism. Here, we investigate a potential role for clathrin in cell-cell adhesion. We observed that the initial steps of AJ formation trigger the phosphorylation of clathrin, and its transient localization at forming cell-cell contacts. Furthermore, we show that clathrin serves as a hub for the recruitment of proteins that are necessary for the actin rearrangements that accompany the maturation of AJs. Using an InlA/E-cadherin chimera, we show that adherent cells expressing the chimera form AJs with cells expressing E-cadherin. We demonstrate that non-adherent cells expressing the InlA chimera, as bacteria, can be internalized by E-cadherin-expressing adherent cells. Together these results reveal that a common clathrin-mediated machinery may regulate internalization and cell adhesion and that the relative mobility of one of the interacting partners plays an important role in the commitment to either one of these processes. | URI: | http://hdl.handle.net/10261/94130 | DOI: | 10.1111/tra.12009 | ISSN: | 1398-9219 | E-ISSN: | 1600-0854 |
Aparece en las colecciones: | (IDAB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
14
checked on 20-mar-2024
SCOPUSTM
Citations
29
checked on 23-abr-2024
WEB OF SCIENCETM
Citations
26
checked on 22-feb-2024
Page view(s)
326
checked on 23-abr-2024
Download(s)
105
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.