Andrew Carter

Andrew Carter

The structural basis of cargo transport by the dynein/dynactin transport machine.
Group Leader page

The health of a neuron depends on long range transport.  My group is interested in dynein, a microtubule motor protein that moves survival factors, protein-aggregates, viruses and many other cargos back along the axon to the neuronal cell body.

Recently cryo-electron microscopy revealed how dynein and its cofactor dynactin come together to form a multi-protein transport machine. The current challenge is to understand how this core complex selects its cargos.

This PhD position will form part of our effort to tackle this problem. It will use structural approaches (cryo-electron microscopy / cryo-electron tomography) on purified cargos together with correlative light and electron microscopy (CLEM) to visualize transport complexes directly within neurons.


References

Reck-Peterson SL, Redwine WB, Vale RD, Carter AP. (2018)
The cytoplasmic dynein transport machinery and its many cargoes.
Nat Rev Mol Cell Biol. 19:382-398.

Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP. (2018)
Cryo-EM shows how dynactin recruits two dyneins for faster movement.
Nature. 554:202-206.

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.
Cell. 169:1303-1314

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.
Science. 347:1441-6.

Schmidt, H., Zalyte, R., Urnavicius, L. and Carter, A.P. (2015)
Structure of human cytoplasmic dynein-2 primed for its power stroke.
Nature. 518:435-8.