Paxillin Found to Be Key Regulator in Focal Adhesions

Scientists from the University of Geneva, in collaboration with the University of Tampere in Finland, have highlighted the key role of a protein called paxillin in focal adhesions. The researchers found that without functional paxillin, cells are unable to attach properly and slip continuously. Their study was published in Communications Biology. 

Recent discoveries suggest that mechanical signals play a major role in cell coordination. "This is why we started to study the ability of cells to decipher and respond to their physical environment," explains researcher Bernhard Wehrle-Haller. "Especially as it could help us to understand how cancer cells use these mechanisms to invade other organs and form metastases."

When cells detect suitable locations, focal adhesions set up to form cellular crampons that anchor the cell to its environment. "But how is this anchoring mechanism regulated? This is what we wanted to find out," explains Marta Ripamonti, first author of the study.

"We knew that this protein [paxillin] played a role in the assembly of focal adhesions, but we didn't expect it to be the key regulator," says Wehrle-Haller. Without functional paxillin, cells are unable to anchor, regardless of the suitability of their environment. In addition, paxillin has also the function of informing the cell that anchoring has taken place correctly, thus transforming a mechanical response into a biological signal that the cell can understand.

These in vitro experiments highlight the major role of paxillin in the migration and adhesion of healthy cells, but they could also be a starting point for a better understanding of cancer development. "It is indeed likely that cancer cells use paxillin to find a place that enhances their survival. Would it be possible to block this mechanism in tumor cells and prevent the formation of metastases? Yes, we think so," concludes Wehrle-Haller.