Tubulin-dependent secretion of S100A6 and cellular signaling pathways activated by S100A6-integrin β1 interaction
Autor: | Anna Filipek, Elzbieta Wyroba, Ewelina Jurewicz |
---|---|
Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Cell signaling PTK2 Cell Cycle Proteins Proximity ligation assay Protein Serine-Threonine Kinases Biology Microtubules S100 Calcium Binding Protein A6 Focal adhesion 03 medical and health sciences Tubulin Calcium-binding protein Cell Adhesion Humans Protein Isoforms Wharton Jelly Cell adhesion Cells Cultured Cell Proliferation Integrin beta1 Mesenchymal Stem Cells Cell Biology Molecular biology Cell biology 030104 developmental biology Gene Expression Regulation p21-Activated Kinases Focal Adhesion Kinase 1 biology.protein Tetradecanoylphorbol Acetate Signal transduction Colchicine Protein Binding Signal Transduction |
Zdroj: | Cellular Signalling. 42:21-29 |
ISSN: | 0898-6568 |
DOI: | 10.1016/j.cellsig.2017.10.004 |
Popis: | S100A6 is a calcium binding protein expressed mainly in fibroblasts and epithelial cells. Interestingly, S100A6 is also present in extracellular fluids. Recently we have shown that S100A6 is secreted by WJMS cells and binds to integrin β1 (Jurewicz et al., 2014). In this work we describe for the first time the mechanism of S100A6 secretion and signaling pathways activated by the S100A6-integrin β1 complex. We show that colchicine suppressed the release of S100A6 into the cell medium, which indicates that the protein might be secreted via a tubulin-dependent pathway. By applying double immunogold labeling and immunofluorescence staining we have shown that S100A6 associates with microtubules in WJMS cells. Furthermore, results obtained from immunoprecipitation and proximity ligation assay (PLA), and from in vitro assays, reveal that S100A6 is able to form complexes with α and β tubulin in these cells, and that the S100A6-tubulin interaction is direct. We have also found that the S100A6 protein, due to binding to integrin β1, activates integrin-linked kinase (ILK), focal adhesion kinase (FAK) and p21-activated kinase (PAK). Our results suggest that binding of S100A6 to integrin β1 affects cell adhesion/proliferation due to activation of ILK and FAK signaling pathways. |
Databáze: | OpenAIRE |
Externí odkaz: |