Welcome to the King Lab

Cen WT
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.

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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 maintaining nuclear envelope structure, which we investigate in vitro using isolated nuclei and force spectroscopy (see Current Research).

In order to understand how LINC complexes dynamically associate with the cytoskeleton, we are identifying the proteins that couple the nucleus to microtubules and reconstituting nuclear-microtubule interfaces in vitro (see Current Research). We are also expanding our experimental approaches to take advantage of tissue culture and mouse models (the latter in collaboration with the laboratory of Valerie Horsley, Ph.D. (MCDB)).

The lab is also initiating a new project to investigate how nuclear envelope membrane proteins regulate recombination. We are particularly interested in how changes in chromatin-nuclear envelope contacts alter recombinatorial potential that may underlie adaptation.