Research Summary
We are interested in mechanochemical coupling in molecular motors, and more generally in mechanotransduction and in the principles and possibilities of motorised molecular self-organisation in biological systems. We focus specifically on the kinesin motors and their microtubule tracks, and are interested in how they read and influence each other's structural dynamics and supramolecular organisation.
Our work is discovery science, aiming to inform the development of new drug therapies for a range of global health problems that includes malaria, cancer, cardiovascular disease, Alzheimers and reproductive disease.
Rob Cross CV
Researcher ID
NCBI bibliography
Warwick Profile
Grant, B.J., Gheorghe, D., Zheng,W., Alonso, M., Huber, G., Dlugosz,M., McCammon, J.A. & Cross, R.A. (2011)
Electrostatically biased binding of kinesin to microtubules
PLOS Biology 9(11) e1001207. Epub 2011 Nov 29
DesGeorges, A., Katsuki, M., Drummond, D.R., Osei, M., Cross, R.A. & Amos, L.A. (2008)
Mal3, the S. pombe homologue of EB1, changes the microtubule lattice
Nature Struc. Mol. Biol. 15 1102-8
Alonso,M.C., Drummond, D.R., Kain, S., Hoeng, J., Amos, L.A. & Cross, R.A. (2007)
An ATP-gate controls tubulin binding by the tethered head of kinesin-1
Science 316 120-123
Carter N.J. & Cross R.A. (2005)
Mechanics of the kinesin step
Nature 435 308-12
Crevel I. M-T. C. Alonso M. & Cross R.A. (2004)
Monastrol stabilises an attached low-friction state of Eg5
Current Biology 14 R411-R412
Doug Drummond | the kinesin binding site on tubulin
The binding site of kinesin-1 on microtubules is not well defined. Alpha and beta tubulin mutants have been created in S. pombe. These will be examined in vivo and in vitro and a map of tubulin amino acids with a significant role in kinesin ATPase activation and motility created.
Miho Katsuki | Reconstituting microtubule dynamics
+TIP proteins form a complex at the plus end of microtubules and regulate the microtubule dynamics. To unravel the +TIPs complex "spatio-temporally", we will track the behaviour of individual or combined purified +TIPs in vitro.
Warwick Profile
Maria Alonso | Moving parts of kinesin
Kinesin is a motor protein that walks processively along a tubulin polymer (road) using one molecule of ATP (petrol) every 8 nm step. As the motor steps between different positions, the moving parts move. To find out how things move, we are making defined mutations in the head, neck and tail.
Neil Venables | Alp14 & Dis1
The rapid polymerisation of microtubules is essential for the dynamic assembly of the microtubule cytoskeleton during different stages of the cell cycle. XMAP215 proteins belong to a highly conserved family that promote microtubule growth by up to a factor of 10. I study the regulation of this process in the two S. pombe TOG/XMAP215 homologues - Alp14 and Dis1.
Mishan Britto | K14 & K5
Cells often oppose the actions of kinesin-5 and kinesin-14. Both motors crosslink microtubules, but K5 moves towards microtubule plus ends, whilst K14 moves towards minus ends. I want to understand more about how each motor influences the other in these mixed-motor situations.
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