Open AccessThe matricellular protein CCN5 regulates podosome function via interaction with integrin α v β 3
Author(s) -
Myers Ronald B.,
Wei Lan,
Castellot John J.
Publication year - 2014
Publication title -
journal of cell communication and signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 44
eISSN - 1873-961X
pISSN - 1873-9601
DOI - 10.1007/s12079-013-0218-2
Subject(s) - podosome , motility , microbiology and biotechnology , integrin , matricellular protein , extracellular matrix , matrix (chemical analysis) , chemistry , cell , cytoskeleton , biology , biochemistry , chromatography
Abstract CCN proteins play crucial roles in cell motility, matrix turnover, and proliferation. In particular, CCN5 plays a role in cell motility and proliferation in several cell types; however, no functional binding proteins for CCN5 have been identified. In this study we report that CCN5 binds to the cell surface receptor integrin α v β 3 in vascular smooth muscle cells. Furthermore, this interaction takes place in podosomes, organelles known to degrade matrix and mediate motility. We show that CCN5 regulates the ability of podosomes to degrade matrix, but does not affect podosome formation. The level of CCN5 present in a podosome negatively correlates with its ability to degrade matrix. Conversely, knockdown of CCN5 greatly enhances the matrix‐degrading ability of podosomes. These findings suggest that the antimotility effects of CCN5 may be mediated through the direct interaction of CCN5 and integrin α v β 3 in podosomes and the concomitant suppression of matrix degradation that is required for cell migration.