I am fascinated by the way nanometer-scale cell components, especially proteins, associate towards building 1,000-fold larger assemblies in cells, for example whole organelles. The assembly processes themselves appear to obey ‘architectural’ restrictions, for example on how to arrange components in space, familiar to anyone who’s ever played with LEGO pieces. At the same time, however, some of the underlying component properties are ‘transmitted’ to the large assembly; the ‘pieces’ are not just passive building blocks but influence what happens around them. I want to understand how this happens.
Over the last few years my group has focused on the assembly process of centriole organelles, which are key for the organisation of animal cells and for cell division. Centrioles are hundreds of nanometer-large, radially-symmetric, polar and chiral structures made entirely of proteins. How do these properties come about? To answer this question, we are ‘dissecting’ centrioles using all the tools in the modern arsenal of structural cell biology, including X-ray crystallography, NMR, electron microscopy, quantitative biophysics and computational simulations. What we learn in this way helps guide both our understanding of centrioles themselves, but also teaches us how to design novel protein-based nanostructures.