Zebrafish genetics and cryo-electron tomography reveal distinct roles of all vertebrate PIH family proteins in axonemal dynein assembly and cilia/flagella motions, assigning specific dynein subtypes to each PIH protein.
Cryo electron tomography provides the first high-resolution 3D axoneme structure from any pathogenic organism, revealing novel structures that support the unique motility of these pathogens through host tissues.
Chaperoning defects in axonemal dynein subunits trigger proteostatic clearance of dynein motors opening up the possibility of trialling proteostasis modulators to treat the motile ciliopathy primary ciliary dyskinesia (PCD).
Calculations of flagellar energetics from beating patterns in sperm reveal that internal dissipation by dynein motors and other passive structures within the flagellum significantly exceeds external hydrodynamic dissipation.
Genetic knock-outs of the dynein-2 intermediate chains reveals that both are essential for correct cilia function and transition zone organization, but play different functions in the assembly of dynein-2 motor and in primary cilia formation.
Building on previous work (Doroquez et al., 2014), it is shown that the centriole core of the basal body degenerates, but the outer wall remodels to template the ciliary axoneme in a subset of C. elegans ciliated sensory neurons.