Advanced microscopy techniques reveal that clusters of Pom1 kinase at the membrane represent the functional unit that shape the concentration gradients and modulate Pom1 mid-cell levels according to cell size.
Proteolysis of lipidated N-terminal peptides that tether Hedgehog morphogens to the surface of source cells is absolutely required for their coupled release and bioactivation in vivo in Drosophila melanogaster.
A new approach using combination of electron microscopy (EM) and high-speed atomic force microscopy (HS-AFM) clearly demonstrates dynamics of dynamin-amphiphysin complexes during membrane constriction and fission suggesting a novel 'clusterase' model of the dynamin-mediated membrane fission.
Release site heterogeneity represents a previously unknown level of structural and functional organization within individual active zones in central synapses, which determines the spatiotemporal dynamics of multi-vesicular release.
Biochemical, single molecule, cell and structural biology studies reveal an interaction between the kinesin-5 tail and motor domains regulating high-force production, which is critical for microtubule sliding motility.