Metastasis begins with the dissemination of cancer cells from the primary tumour; this requires the remodelling and degradation of the extracellular matrix (ECM) and is mediated mostly by the matrix metalloprotease MT1-MMP, which is delivered to invadopodia from Rab7-containing endolysosomal compartments. However, it is unclear how MT1-MMP is recycled from the plasma membrane (PM) and sorted into these reservoirs. Flotillin 1 and flotillin 2 are ubiquitous membrane-associated proteins that are upregulated in many invasive cancers. This prompted Cécile Gauthier-Rouvière and co-workers (Planchon et al., 2018) to investigate their molecular role in invasive carcinoma and sarcoma cell lines. They show here that flotillin 1 and flotillin 2, which are upregulated in these cells, colocalise with MT1-MMP in endocytic vesicles that emerge from the PM and are trafficked together to a non-proteolytic endolysosmal compartment. Accordingly, knockdown of flotillins reduces the accumulation of MT1-MMP in this compartment, as well as its subsequent secretion, thus reducing invasion. By using an in vitro MT1-MMP uptake assay, the authors further demonstrate that the upregulation of flotillins is sufficient to induce MT1-MMP endocytosis, delineating a clathrin-independent route for MT1-MMP internalisation towards endolysosomal reservoirs. These findings thus not only describe a gain-of-function role of upregulated flotillins in MT1-MMP trafficking in invasive cancer but also point to possible new routes for therapeutic intervention.