Proteomic analysis of Tks5 interactome to identify common marker of all types of invadosomes.

ABSTRACT: Invasion of the extracellular matrix is needed for physiological events such as wound healing but is also required at different stages of the metastatic process. The ability to progress and invade through the extracellular matrix is a characteristic shared by both normal and cancer cells through the formation of structures called invadosomes. These invadosomes are dynamic structures that can adopt different organizations such as rosettes, dots or can be reorganized along the type I collagen into linear invadosomes. In this study, we used the universal marker of invadosomes Tks5 to identify common features in the different organizations. We used Tks5 co-immunoprecipitation coupled with mass spectrometry analysis that allowed us to identify a translation machinery in all types of organization and in particular the protein Eif4b. We showed that Eif4b colocalized with Tks5 in dots, rosettes and linear invadosomes. Thanks to functional tests, we showed for the first time that EIF4B and the translation are involved in the degradation function of all types of invadosomes. Finally, we also identified the presence of an endoplasmic reticulum at the level of rosette that colocalizes with Tks5. In summary, we provided a molecular characterization of the different types of invadosomes, in normal and cancerous cells, thanks to the common marker Tks5. Moreover, we demonstrated for the first time the presence of a translation machinery in linear invadosomes essential to their degradation function and more generally in all types of invadosomes. We also identified the colocalization of endoplasmic reticulum with Tks5 in rosette. The combination of molecular and structural analysis of the different invadosomes organization allowed us to better understand the composition of these invasive structures.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Dupuy Jean-William  

LAB HEAD: Frederic Saltel

PROVIDER: PXD046512 | Pride | 2025-11-26

REPOSITORIES: Pride