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Up-regulation of flotillins, new marker of metastatic development, induces cell invasion and metastatic development D. Planchon, E. R. Morris, F. Comunale [et.al.]

Contributor(s): Planchon, D | Genest, M | Comunale, F | Vacher, Sophie | Biche, I | Denisov, Evgeny V | Tashireva, Liubov A | Perelmuter, Vladimir M | Linder, S | Morris, E. R | Chavrier, Ph | Bodin, S | Gauthier-Rouvière, CMaterial type: ArticleArticleSubject(s): флотилины | опухолевая инвазия | онкомаркеры | метастазированиеGenre/Form: статьи в сборниках Online resources: Click here to access online In: The 22nd International Charles Heidelberger symposium on cancer research : proceedings of the International symposium, 17-19 September 2018 P. 87-88Abstract: Flotillin 1 and 2 are two ubiquitous, highly conserved and related proteins present in many cellular membrane compartments. They exist as hetero-tetramers associated with specific caveolinindependent membrane microdomains rich in cholesterol and glycosphingolipids. Flotillin heterotetramers assemble in large oligomers to form molecular membrane scaffolds known to participate in membrane proteins clustering [1]. When overexpressed, as it occurs in many invasive carcinoma and sarcoma, they induce the formation of plasma membrane invaginations and of intracellular vesicles and modify the trafficking of several cargos; promoting the Upregulated Flotillin-Induced Trafficking (UFIT) pathway [2‑3].Flotillin overexpression is detected in many invasive carcinoma and sarcoma and is a marker of poor prognosis associated with a higher metastatic risk [4‑8]. How flotillins participate in the acquisition of invasive and metastatic properties remains to be determined. Our study aims at identifying how the UFIT pathway influences the membrane remodeling and modifies the trafficking of cargo leading to the acquisition of invasive properties. We show that flotillins downregulation in invasive cancer cells dramatically inhibit their invasive properties as monitored in vitro using a 3D-collagen invasion assay and in vivo using zebrafish xenografts. Reciprocally, ectopic up-regulation of flotillins in non-tumoral cells is sufficient to induce their invasive behavior in vitro and in vivo. We show that flotillins are critical regulators of the trafficking of several cargo amongst them MT1-MMP, a key metalloproteinase responsible for the proteolytic activity of invadopodia [9].
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Flotillin 1 and 2 are two ubiquitous, highly conserved and related proteins present in many
cellular membrane compartments. They exist as hetero-tetramers associated with specific caveolinindependent
membrane microdomains rich in cholesterol and glycosphingolipids. Flotillin heterotetramers
assemble in large oligomers to form molecular membrane scaffolds known to participate
in membrane proteins clustering [1]. When overexpressed, as it occurs in many invasive carcinoma
and sarcoma, they induce the formation of plasma membrane invaginations and of intracellular
vesicles and modify the trafficking of several cargos; promoting the Upregulated Flotillin-Induced
Trafficking (UFIT) pathway [2‑3].Flotillin overexpression is detected in many invasive carcinoma and sarcoma and is a marker
of poor prognosis associated with a higher metastatic risk [4‑8]. How flotillins participate in the
acquisition of invasive and metastatic properties remains to be determined.
Our study aims at identifying how the UFIT pathway influences the membrane remodeling and
modifies the trafficking of cargo leading to the acquisition of invasive properties.
We show that flotillins downregulation in invasive cancer cells dramatically inhibit their invasive
properties as monitored in vitro using a 3D-collagen invasion assay and in vivo using zebrafish
xenografts. Reciprocally, ectopic up-regulation of flotillins in non-tumoral cells is sufficient to
induce their invasive behavior in vitro and in vivo. We show that flotillins are critical regulators
of the trafficking of several cargo amongst them MT1-MMP, a key metalloproteinase responsible
for the proteolytic activity of invadopodia [9].

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