Focal adhesion articles from across Nature Portfolio

The molecular mechanism of how Mdm2 regulates cell migration remains to be elucidated. Here the authors report the role of Mdm2-x complexes, independent of p53, modulates the expression of Sprouty4 and regulates the cellular processes by decreasing the metastatic capability of cancer cells.

Focal adhesions are force resisting, highly dynamic protein clusters. Here, the authors show that focal adhesion proteins undergo liquid-liquid phase separation on lipid membranes, shedding light on their unique properties.

PI3 kinase is known to promote cell migration through its catalytic activity. Here, the authors show that the kinase also induces endocytosis through a non-catalytic pathway that actually decreases migratory speed and persistence, revealing a more subtle regulation of motility.

Regulation of endothelial barrier function is critical to physiological function of the vasculature, which must dynamically change in many physiologic and pathologic settings. A new study emphasizes the complex relationship between VE-cadherin phosphorylation and vascular leak and the critical role of the tyrosine kinase Yes in this process.

While integrin-based adhesions are thought to underlie many aspects of cell response to localized tension, another matrix receptor, syndecan-4, has now been shown to act as a mechanosensor, which triggers cell-wide integrin activation and adhesion reinforcement.

Integrin-based focal adhesions integrate biochemical and biomechanical signals from the extracellular matrix and the actin cytoskeleton. The combination of three-dimensional super-resolution imaging and loss- or gain-of-function protein mutants now links the nanoscale dynamic localization of proteins to their activation and function within focal adhesions.