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A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells

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dc.contributor Háskóli Íslands
dc.contributor University of Iceland
dc.contributor.author Thuault, Sylvie
dc.contributor.author Mamelonet, Claire
dc.contributor.author Salameh, Joëlle
dc.contributor.author Ostacolo, Kevin
dc.contributor.author Chanez, Brice
dc.contributor.author Salaün, Danièle
dc.contributor.author Baudelet, Emilie
dc.contributor.author Audebert, Stéphane
dc.contributor.author Camoin, Luc
dc.contributor.author Badache, Ali
dc.date.accessioned 2020-10-27T15:57:51Z
dc.date.available 2020-10-27T15:57:51Z
dc.date.issued 2020-04-22
dc.identifier.citation Thuault, S., Mamelonet, C., Salameh, J. et al. A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells. Sci Rep 10, 6787 (2020). https://doi.org/10.1038/s41598-020-63926-4
dc.identifier.issn 2045-2322
dc.identifier.uri https://hdl.handle.net/20.500.11815/2144
dc.description Publiher's version (útgefin grein)
dc.description.abstract Metastatic progression is the leading cause of mortality in breast cancer. Invasive tumor cells develop invadopodia to travel through basement membranes and the interstitial matrix. Substantial efforts have been made to characterize invadopodia molecular composition. However, their full molecular identity is still missing due to the difficulty in isolating them. To fill this gap, we developed a non-hypothesis driven proteomic approach based on the BioID proximity biotinylation technology, using the invadopodia-specific protein Tks5α fused to the promiscuous biotin ligase BirA* as bait. In invasive breast cancer cells, Tks5α fusion concentrated to invadopodia and selectively biotinylated invadopodia components, in contrast to a fusion which lacked the membrane-targeting PX domain (Tks5β). Biotinylated proteins were isolated by affinity capture and identified by mass spectrometry. We identified known invadopodia components, revealing the pertinence of our strategy. Furthermore, we observed that Tks5 newly identified close neighbors belonged to a biologically relevant network centered on actin cytoskeleton organization. Analysis of Tks5β interactome demonstrated that some partners bound Tks5 before its recruitment to invadopodia. Thus, the present strategy allowed us to identify novel Tks5 partners that were not identified by traditional approaches and could help get a more comprehensive picture of invadopodia molecular landscape.
dc.description.sponsorship We thank D. Isnardon and M. Rodriguez (CRCM Microscopy Platform) for support and S.A. Courtneidge, K.J. Roux and C. Lachaud for sharing reagents. This work was supported by Canceropôle Provence-Alpes-Côte d’Azur (PACA), Institut National du Cancer, Conseil Régional PACA and Site de Recherche Intégrée sur le Cancer (SIRIC). Proteomic analyses were performed at the mass spectrometry facility of Marseille Proteomics supported by IBISA (Infrastructures Biologie Santé et Agronomie), Plateforme Technologique Aix-Marseille, Canceropôle PACA, Région Sud Provence-Alpes-Côte d’Azur, Fonds Européen de Développement Régional (FEDER) and Plan Cancer.
dc.format.extent 6787
dc.language.iso en
dc.publisher Springer Science and Business Media LLC
dc.relation.ispartofseries Scientific Reports;10(1)
dc.rights info:eu-repo/semantics/openAccess
dc.subject Breast cancer
dc.subject Cell biology
dc.subject Protein–protein interaction networks
dc.subject Brjóstakrabbamein
dc.subject Frumulíffræði
dc.title A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells
dc.type info:eu-repo/semantics/article
dcterms.license Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
dc.description.version Peer Reviewed
dc.identifier.journal Scientific Reports
dc.identifier.doi 10.1038/s41598-020-63926-4
dc.relation.url https://www.nature.com/articles/s41598-020-63926-4
dc.contributor.department Læknadeild (HÍ)
dc.contributor.department Faculty of Medicine (UI)
dc.contributor.department Lífvísindasetur (HÍ)
dc.contributor.department Biomedical Center (UI)
dc.contributor.school Heilbrigðisvísindasvið (HÍ)
dc.contributor.school School of Health Sciences (UI)

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