Time lapse of wild type centromere (green) and Sad1 (red)
Macromolecular complexes embedded in the nuclear envelope physically couple the cytoskeleton to the nucleus. These molecular bridges (LINC complexes) allow the cytoskeleton to regulate nuclear position within the cell. In addition, they provide a mechanism for signals to be mechanically transduced between the cytoplasm and nucleus. More broadly, nuclear envelope membrane proteins serve to compartmentalize chromatin within the nucleus.
Our lab primarily uses the fission yeast model, Schizosaccharomyces pombe, to investigate LINC complex function. Using cell biological techniques, we are interested in understanding when, how and why chromatin regions associate with the nuclear aspect of LINC complexes. In particular, we are interested in how LINC complexes and cytoskeletal forces serve as inputs to the processes of DNA repair (see Current Research), telomere maintenance and general chromatin mobility. We are also investigating the physical role that chromatin plays in defining nuclear mechanics, which we investigate in vitro using isolated nuclei and force spectroscopy (see Current Research). We also investigate the role(s) of the LINC complex in tissue-level mechanics in mammalian systems in collaboration with the laboratory of Valerie Horsley, Ph.D. (MCDB).
The lab has also recently founded a new project to investigate how the compartment of the nuclear envelope influences recombination. We are particularly interested in how changes in chromatin-nuclear envelope contacts alter recombinatorial potential that may underlie adaptation.