Molecular Biology & Biochemistry
Our laboratory seeks to understand several aspects of the eukaryotic cytoskeleton, a dynamic and extensive cellular protein network composed mostly of actin filaments and tubulin-containing microtubules.
One area of research we are pursuing is to decipher the roles that molecular chaperones play in the folding of actin and tubulin proteins. Three players of particular relevance include the chaperonin CCT, and two cofactors, the jellyfish-shaped prefoldin chaperone and the phosducin-like proteins 2 and 3.
Another focus of our studies involves identifying and characterising proteins found within the cilium, an evolutionarily ancient microtubule-based organelle. Using the nematode C. elegans, we study intraflagellar transport, a kinesin- and dynein-dependent transport process necessary for the formation and maintenance of the complex ciliary structure. Cilia are found in a large proportion of unicellular organisms, and in humans, motile and non-motile (primary) cilia play important roles in moving fluids or sensing the extracellular environment. As part of these studies, we probe the molecular basis of some human disorders that arise from ciliary dysfunction, including Bardet-Biedl Syndrome and Meckel syndrome. Genetic disorders involving cilia are characterised by a wide range of ailments, such as obesity, kidney and heart anomalies, blindness, and neurosensory impairment. We are also attempting to understand at the molecular how cilia modulate signaling processes that affect development and physiology. Also of interest to us is how proteins associated with cilia function may participate in the intracellular trafficking of proteins at the centrosome, the microtubule organising centre of cells.