What is it about?
We 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). We showed 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. Results obtained from immunoprecipitation, 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.
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Why is it important?
Our results provide evidence that S100A6 is secreted from WJMS cells via a tubulin–dependent pathway and that it "decorates" microtubules in these cells. S100A6 was also shown to bind directly to tubulin using in vitro assays.
Perspectives
In the present work we established a tubulin-dependent mechanism of S100A6 secretion by WJMS cells and signaling pathways activated by the S100A6-integrin β1 complex in these cells.
Professor Elzbieta Wyroba
Nencki Institute of Experimental Biology
Read the Original
This page is a summary of: Tubulin-dependent secretion of S100A6 and cellular signaling pathways activated by S100A6-integrin β1 interaction, Cellular Signalling, January 2018, Elsevier,
DOI: 10.1016/j.cellsig.2017.10.004.
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