title: Physiological type I collagen organization induces the formation of a novel class of linear invadosomes.
abstract: Invadosomes are F-actin structures capable of degrading the matrix through the activation of matrix metalloproteases. As fibrillar type I collagen promotes pro-matrix metalloproteinase 2 activation by membrane type 1 matrix metalloproteinase, we aimed at investigating the functional relationships between collagen I organization and invadosome induction. We found that fibrillar collagen I induced linear F-actin structures, distributed along the fibrils, on endothelial cells, macrophages, fibroblasts, and tumor cells. These structures share features with conventional invadosomes, as they express cortactin and N-WASP and accumulate the scaffold protein Tks5, which proved essential for their formation. On the basis of their ability to degrade extracellular matrix elements and their original architecture, we named these structures "linear invadosomes." Interestingly, podosomes or invadopodia were replaced by linear invadosomes upon contact of the cells with fibrillar collagen I. However, linear invadosomes clearly differ from classical invadosomes, as they do not contain paxillin, vinculin, and β1/β3 integrins. Using knockout mouse embryonic fibroblasts and RGD peptide, we demonstrate that linear invadosome formation and activity are independent of β1 and β3 integrins. Finally, linear invadosomes also formed in a three-dimensional collagen matrix. This study demonstrates that fibrillar collagen I is the physiological inducer of a novel class of invadosomes.
authors: INSERM, U1053, F-33076 Bordeaux, France.
authors: Amélie
authors: A
authors: Juin
authors: Clotilde
authors: C
authors: Billottet
authors: Violaine
authors: V
authors: Moreau
authors: Olivier
authors: O
authors: Destaing
authors: Corinne
authors: C
authors: Albiges-Rizo
authors: Jean
authors: J
authors: Rosenbaum
authors: Elisabeth
authors: E
authors: Génot
authors: Frédéric
authors: F
authors: Saltel
mesh_terms: D000199:Actins / Q000378:metabolism; D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002460:Cell Line; D024042:Collagen Type I / Q000378:metabolism* / Q000648:ultrastructure*; D006224:Cricetinae; D005109:Extracellular Matrix / Q000378:metabolism*; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D019012:Integrin beta1 / Q000378:metabolism; D039661:Integrin beta3 / Q000378:metabolism; D051379:Mice; D018345:Mice, Knockout; D009842:Oligopeptides / Q000494:pharmacology; D013552:Swine; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal / Q000378:metabolism
chemical_list: D000199:Actins; D033942:Adaptor Proteins, Vesicular Transport; D024042:Collagen Type I; D019012:Integrin beta1; D039661:Integrin beta3; D009842:Oligopeptides; C478582:SH3PXD2A protein, human; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal; C047981:arginyl-glycyl-aspartic acid