期刊
MOLECULAR BIOLOGY OF THE CELL
卷 23, 期 2, 页码 297-309出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E11-07-0594
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资金
- Ministere de l'Enseignement Superieur et de la Recherche
- La Ligue Nationale contre le Cancer
- Association pour la Recherche sur le Cancer/Institut National du Cancer
- Equipe Labellisee
- [ANR-06-BLAN-0362]
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 beta 1/beta 3 integrins. Using knockout mouse embryonic fibroblasts and RGD peptide, we demonstrate that linear invadosome formation and activity are independent of beta 1 and beta 3 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.
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