Caco-2 cells labeled for tight junction molecule cingulin (green), actin (red), vinculin (pink) and DNA (blue).
Epithelial cells growing on a patterned adhesive surface with the shape of the Weizmann Institute tree.
Desmosomes in mouse tongue epithelium (by transmission electron microscope).
Porcine aortic endothelial cell, double-labeled for actin (green) and phospho-tyrosine (red).
“Molecular composition map” of focal adhesions and stress fibers.
Myeloma cancer cell responding to shear flow (by scanning electron microscope).
Or-Yam Revach
Molecular composition and structural organization of adhesion proteins in invadopodia
Invadopodia are actin-rich membrane protrusions of cancer cells that form an attachment to and degradation of the ECM(extra cellular matrix). The invadosome structure has two distinct parts: the core is an actin-rich column containing proteins involved in actin nucleation and regulation, such as Wiskott–Aldrich syndrome protein (WASP), Arp2/3 cortactin, cofilin and formins. The second part is adhesive ring composed of integrin receptors and integrin-associated proteins, is a multi-molecular complex surrounding the core.
Data are relatively plentiful regarding the adhesion proteins in the Src-induced invadosome and podosome type invadosomes, but less is known about the molecular composition and structural organization of the adhesive ring in invadopodia.
We are interested in the importance of the adhesion proteins for invadopodia formation and function. Our study focuses on dynamic research in live cell-imaging and protein organization and localization in high-resolution microscopy.
Figure Legend
In the figure, A375MM cells co-stained for the invadopodia core marker TKS5, and an adhesion protein (either paxillin or vinculin) that forms a ring around the core.