The cytoplasmic dynein complex, along with its cofactor dynactin and other regulatory proteins, acts as a motor that moves along microtubules. Among its many functions, dynein organises membraneous compartments, gathers up misfolded proteins, carries viruses and plays key roles in cell division and replication.

Despite playing such a prominent and crucial role in numerous biological and disease processes, until recently very little structural information was known for cytoplasmic dynein. Challenges such as its large size, complexity and low abundance mean that it represents one of the major unexplored and exciting frontiers in structural biology.

The goal of our group is to use a combination of X-ray crystallography, cryo-electron microscopy and advanced single molecule techniques to further our understanding of the structure and mechanism of the dynein mega complex. This will allow us to answer questions such as how it moves along microtubules, how it is regulated and how it interacts with cargos. The long-term goal is that this information will aid the development of therapeutics that will block certain dynein functions (such as transport of viruses) without inhibiting the whole motor.