Reduced PaxillinB Localization to Cell-substrate Adhesions Promotes Cell Migration in

Many cells adhere to extracellular matrix for efficient cell migration. This adhesion is mediated by focal adhesions, a protein complex linking the extracellular matrix to the intracellular cytoskeleton. Focal adhesions have been studied extensively in mesenchymal cells, but recent research in physiological contexts and amoeboid cells suggest focal adhesion regulation differs from the mesenchymal focal adhesion paradigm. We used to uncover new mechanisms of focal adhesion regulation, as are amoeboid cells that form focal adhesion-like structures for migration. We show that PaxillinB, the homologue of Paxillin, localizes to dynamic focal adhesion-like structures during migration. Unexpectedly, reduced PaxillinB recruitment to these structures increases cell migration. Quantitative analysis of focal adhesion size and dynamics show that lack of PaxillinB recruitment to focal adhesions does not alter focal adhesion size, but rather increases focal adhesion turnover. These findings are in direct contrast to Paxillin function at focal adhesions during mesenchymal migration, challenging the established focal adhesion model.