Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.

Flotillin-1 and flotillin-2 are two homologous, membrane raft associated proteins. Although it has been reported that flotillins are involved in cell adhesion processes and play a role during breast cancer progression, thus making them interesting future therapeutic targets, their precise function h...

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Autores principales:	Nina Kurrle, Frauke Völlner, Rüdiger Eming, Michael Hertl, Antje Banning, Ritva Tikkanen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fb63a06146ca4b549cf7cfe54edf938b
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spelling	oai:doaj.org-article:fb63a06146ca4b549cf7cfe54edf938b2021-11-18T08:39:20ZFlotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.1932-620310.1371/journal.pone.0084393https://doaj.org/article/fb63a06146ca4b549cf7cfe54edf938b2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24391950/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Flotillin-1 and flotillin-2 are two homologous, membrane raft associated proteins. Although it has been reported that flotillins are involved in cell adhesion processes and play a role during breast cancer progression, thus making them interesting future therapeutic targets, their precise function has not been well elucidated. The present study investigates the function of these proteins in cell-cell adhesion in non-malignant cells. We have used the non-malignant epithelial MCF10A cells to study the interaction network of flotillins within cell-cell adhesion complexes. RNA interference was used to examine the effect of flotillins on the structure of adherens junctions and on the association of core proteins, such as E-cadherin, with membrane rafts. We here show that the cadherin proteins of the adherens junction associate with flotillin-2 in MCF10A cells and in various human cell lines. In vitro, flotillin-1 and flotillin-2 directly interact with γ-catenin which is so far the only protein known to be present both in the adherens junction and the desmosome. Mapping of the interaction domain within the γ-catenin sequence identified the Armadillo domains 6-8, especially ARM domain 7, to be important for the association with flotillins. Furthermore, depletion of flotillins significantly influenced the morphology of the adherens junction in human epithelial MCF10A cells and altered the association of E-cadherin and γ-catenin with membrane rafts. Taken together, these observations suggest a functional role for flotillins, especially flotillin-2, in cell-cell adhesion in non-malignant epithelial cells.Nina KurrleFrauke VöllnerRüdiger EmingMichael HertlAntje BanningRitva TikkanenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e84393 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nina Kurrle Frauke Völlner Rüdiger Eming Michael Hertl Antje Banning Ritva Tikkanen Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
description	Flotillin-1 and flotillin-2 are two homologous, membrane raft associated proteins. Although it has been reported that flotillins are involved in cell adhesion processes and play a role during breast cancer progression, thus making them interesting future therapeutic targets, their precise function has not been well elucidated. The present study investigates the function of these proteins in cell-cell adhesion in non-malignant cells. We have used the non-malignant epithelial MCF10A cells to study the interaction network of flotillins within cell-cell adhesion complexes. RNA interference was used to examine the effect of flotillins on the structure of adherens junctions and on the association of core proteins, such as E-cadherin, with membrane rafts. We here show that the cadherin proteins of the adherens junction associate with flotillin-2 in MCF10A cells and in various human cell lines. In vitro, flotillin-1 and flotillin-2 directly interact with γ-catenin which is so far the only protein known to be present both in the adherens junction and the desmosome. Mapping of the interaction domain within the γ-catenin sequence identified the Armadillo domains 6-8, especially ARM domain 7, to be important for the association with flotillins. Furthermore, depletion of flotillins significantly influenced the morphology of the adherens junction in human epithelial MCF10A cells and altered the association of E-cadherin and γ-catenin with membrane rafts. Taken together, these observations suggest a functional role for flotillins, especially flotillin-2, in cell-cell adhesion in non-malignant epithelial cells.
format	article
author	Nina Kurrle Frauke Völlner Rüdiger Eming Michael Hertl Antje Banning Ritva Tikkanen
author_facet	Nina Kurrle Frauke Völlner Rüdiger Eming Michael Hertl Antje Banning Ritva Tikkanen
author_sort	Nina Kurrle
title	Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
title_short	Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
title_full	Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
title_fullStr	Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
title_full_unstemmed	Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
title_sort	flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/fb63a06146ca4b549cf7cfe54edf938b
work_keys_str_mv	AT ninakurrle flotillinsdirectlyinteractwithgcateninandregulateepithelialcellcelladhesion AT fraukevollner flotillinsdirectlyinteractwithgcateninandregulateepithelialcellcelladhesion AT rudigereming flotillinsdirectlyinteractwithgcateninandregulateepithelialcellcelladhesion AT michaelhertl flotillinsdirectlyinteractwithgcateninandregulateepithelialcellcelladhesion AT antjebanning flotillinsdirectlyinteractwithgcateninandregulateepithelialcellcelladhesion AT ritvatikkanen flotillinsdirectlyinteractwithgcateninandregulateepithelialcellcelladhesion
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Flotillins directly interact with γ-catenin and regulate epithelial cell-cell adhesion.

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