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

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


Title: A proximity-labeling proteomic approach to investigate invadopodia molecular landscape in breast cancer cells
Author: Thuault, Sylvie
Mamelonet, Claire
Salameh, Joëlle
Ostacolo, Kevin   orcid.org/0000-0003-2592-7980
Chanez, Brice
Salaün, Danièle
Baudelet, Emilie
Audebert, Stéphane
Camoin, Luc
Badache, Ali
Date: 2020-04-22
Language: English
Scope: 6787
University/Institute: Háskóli Íslands
University of Iceland
School: Heilbrigðisvísindasvið (HÍ)
School of Health Sciences (UI)
Department: Læknadeild (HÍ)
Faculty of Medicine (UI)
Lífvísindasetur (HÍ)
Biomedical Center (UI)
Series: Scientific Reports;10(1)
ISSN: 2045-2322
DOI: 10.1038/s41598-020-63926-4
Subject: Breast cancer; Cell biology; Protein–protein interaction networks; Brjóstakrabbamein; Frumulíffræði
URI: https://hdl.handle.net/20.500.11815/2144

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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

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.

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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/.

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