Rob

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 and in synthetic nanosystems.


My laboratory focuses specifically on the mechanochemistry of kinesins and microtubules. We are interested in particular in how kinesin motors and their microtubule tracks read and feed back upon each other's organization and mechanochemical status, both directly, and via sets of associated proteins.


Our work is basic science, but we aim to harness our findings to illuminate routes to better medicines.


Rob Cross CV

Selected Publications

 

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


lab members & projects

DougDoug 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.

 

MihoMiho Katsuki | Reconstituting microtubule dynamics

+TIP proteins form a complex at the plus end of microtubules and regulate the microtubule dynamics. The proteins forming the complex depend on microtubule-growth state and cell cycle. To unravel the +TIPs complex "spatio-temporally", we will track the behaviour of individual or combined purified +TIPs-Qdot fusion proteins in vitro.

 

MariaMaria 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.

 

FraukeFrauke Hussmann | Alp14 & Dis1

There are two XMAP215 family microtubule binding proteins, in S. pombe, Alp14 and Dis1. I want to express and purify these proteins and find out how they modify the assembly of S. pombe tubulin.

 

 

MishanMishan 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.

 

Past members here

funding sources

 

mccc

aicr