The structural basis of cargo transport by the dynein/dynactin transport machine.
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Movement is one of the defining characteristics of life and at the sub-cellular level many motions are driven by motor proteins walking along the actin and microtubule tracks that extend throughout the cytoplasm. My group is interested in dynein: a multi-protein complex that is arguably one of the most interesting and least studied of all these motors.
Work on dynein has until recently been hindered by its large size and complexity. Now, however, the tools are becoming available that are allowing us to tackle its structure and address questions such as how it generates movement, how it interacts specifically with the many different cargos in carries and how it can be hijacked by viruses.
This PhD project will use structural approaches (cryo-electron microscopy and cryo-electron tomography), together with protein biochemistry and single molecule fluorescence microscopy to investigate how dynein selects the cargos it carries.
Zhang, K., Foster, H.E., Rondelet, A., Lacey, S.E., Bahi-Buisson, N., Bird, A.W. and Carter, A.P. (2017)
Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated.
Urnavicius, L., Zhang, K., Diamant, A.G., Motz, C., Schlager, M.A., Yu, M., Patel, N.A., Robinson, C.V. and Carter, A.P. (2015)
The structure of the dynactin complex and its interaction with dynein.
Schmidt, H., Zalyte, R., Urnavicius, L. and Carter, A.P. (2015)
Structure of human cytoplasmic dynein-2 primed for its power stroke.
Schlager, M.A., Hoang, H.T., Urnavicius, L., Bullock, S.L. and Carter, A.P. (2014)
In vitro reconstitution of a highly processive recombinant human dynein complex.
EMBO J. 33(17):1855-68.