The structure of the Ana2 Central Coiled-Coil Domain provides insight into how centriolar cartwheel components may be recruited and assembled, and indicates that cartwheel assembly involves more than just SAS-6 oligomerisation.
Intersectin counterparts in yeast recruit WASP and WIP to endocytic sites to establish a robust multivalent SH3 domain-PRM interaction network which gives actin assembly onset a switch-like behavior in vivo.
Building on previous work (Conduit et al., 2014), and contrary to what was previously thought, it is shown that key centrosomal proteins are not recruited to centrosomes as part of large multi-protein assemblies.
Newly discovered interaction between fission yeast SPB and animal centriole components reveals that pericentrin not only functions as a microtubule-nucleator, but also promotes centriole assembly in animals.
Single-molecule TIRF microscopy, biochemical assays and mathematical modeling demonstrate how actin-branch nucleation by the Arp2/3 complex is coordinately regulated by two biochemically distinct activators.
A genetic screen and live cell imaging show that a newly identified coiled-coil protein called SAS-7 is the earliest acting factor in centriole assembly yet identified in the roundworm Caenorhabditis elegans.