Ubiquitination is accomplished through the sequential actions of ubiquitin-activating (E1) enzymes, ubiquitin-conjugating (E2) enzymes, and ubiquitin ligases (E3).

web_ubiCurrent projects in our lab are directed at both E2 and E3 enzymes and address the following key questions:

  • How do E3 enzymes recognize and modify target proteins?
  • How do E3 enzymes achieve linkage specificity in ubiquitin chain formation?
  • How are E2 and E3 enzymes regulated? How does the formation of supramolecular complexes impact the activities of E2 and E3 enzymes?
  • How does ubiquitination crosstalk with other types of posttranslational modifications, such as phosphorylation?

To answer these questions we use a variety of techniques including X-ray crystallography, NMR spectroscopy, computational tools, biophysical measurements, biochemical and cell biological assays.