Atomic force microscopy (AFM) provides a less invasive approach to characterize mechanical properties of single cells and multicellular systems without any treatment. A variety of AFM nanoindentation techniques has been developed allowing to quantify the mechanical properties of cells and to explore the spatial and/or temporal dynamics of single cell stiffness in multicellular systems such as cell monolayer and developing embryo. This commentary addresses the reliability and limitations of the present AFM to obtain the universal and specific features of cell mechanical properties in multicellular systems.
Many structural subunits of the bacterial flagellum are transported to the distal end of the growing flagellar structure via a unique and specific protein export apparatus to construct a supramolecular motility machine on the cell surface. The flagellar export apparatus is composed of a transmembrane export gate complex and a cytoplasmic ATPase ring complex. The export gate complex utilizes the transmembrane electrical potential difference of protons, which is defined as membrane voltage, as the energy source to drive proton-coupled protein export. In this review, we describe our current understanding of the membrane voltage-dependent activation mechanism of the export gate complex.
Cellular membranes are composed of a complex lipid mixture that forms a membrane lipid environment, which establishes organelle identity and contributes to organelle function. Yet, how small-scale membrane environment organizes physiological events remains obscure. Our recent study shows that a nanoscale membrane lipid environment created by Osh lipid transfer proteins drives phosphatidylinositol 4-phosphate 5-kinase (PIP5K) activity and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] synthesis. In addition, we demonstrate that an amphipathic α-helix conserved in PIP5K serves as a lipid sensor for the nanoscale lipid environment.