Thomas Surrey

Synthetic & Systems Biochemistry of the Microtubule Cytoskeleton Laboratory

The cytoskeleton is essential for the internal organisation of eukaryotic cells. Microtubules, motor proteins and other microtubule-associated proteins form a mechano-chemical network that determines the dynamic and adaptable nature of intracellular order. Distinct forms of cytoskeletal architectures are required for correct cell division and cell differentiation. How the components of the microtubule cytoskeleton work together as a system is not understood.

We address these questions using a combination of physical biochemistry and quantitative cell biology. Advanced fluorescence microscopy (down to the single molecule level), in vitro reconstitutions of dynamic cytoskeleton behaviour, microfabrications and microfluidics, as well as eukaryotic cell culture are important tools in our research.

Our aim is to understand in quantitative terms the molecular mechanisms underlying cytoskeleton architecture and function. We focus on the question of how the microtubule cytoskeleton organises itself within the boundary of the cellular membrane and how the mitotic spindle assembles and functions during cell division. We aim at being able to predict the behaviour of the dynamic cytoskeleton based on quantitative knowledge of the properties of its constituents.

In the future, we will address the following questions:

  • How do single molecules of the microtubule cytoskeleton behave in living cells?
  • Can an artificial cytoskeleton be constructed from purified components and inform us about complex cytoskeleton functionalities?
  • How do biochemistry and mechanics integrate within the cytoskeleton?
Figure 1

Figure 1. The Microtubule Cytoskeleton. (Click to view larger image)

 

Selected publications

Duellberg C., Cade N.I., Holmes D., Surrey T. (2016) The size of the EB cap determines instantaneous microtubule stability. Elife 5, e13470.

Roostalu J., Cade N.I., Surrey T. (2015) Complementary activities of TPX2 and chTOG constitute an efficient importin-regulated microtubule nucleation module. Nat. Cell Biol. 17, 1422-1434. 

Duellberg C, Trokter M, Jha R, Sen I, Steinmetz MO, Surrey T. (2014) Reconstitution of a hierarchical +TIP interaction network controlling microtubule end tracking of the human dynein complex. Nat. Cell. Biol. 16, 804-811.

Maurer SP, Fourniol FJ, Bohner G, Moores CA, Surrey T. (2012) EBs recognize a nucleotide-dependent structural cap at growing microtubule ends. Cell 149, 371-382

Trokter M, Mücke N, Surrey T. (2012) Reconstitution of the human cytoplasmic dynein complex. Proc Natl Acad Sci U S A. 109, 20895-20900.

Roostalu J, Hentrich C, Bieling P, Telley IA, Schiebel E, Surrey T. (2011) Directional Switching of the Kinesin Cin8 Through Motor Coupling. Science 332, 94-99.

Bieling P, Telley IA, Surrey T. (2010) A minimal midzone protein module controls formation and length of antiparallel microtubule overlaps. Cell 142, 420-432.

Bieling P, Laan L, Schek H, Munteanu EL, Sandblad L, Dogterom M, Brunner D, Surrey T. (2007) Reconstitution of a microtubule plus-end tracking system in vitro. Nature 450, 1100-1105.

Thomas Surrey

thomas.surrey@crick.ac.uk
+44 (0)20 379 62044

  • Qualifications and history
  • 1995 PhD, University of Tuebingen and Max-Planck Institute for Biology, Germany
  • 1995 Postdoctoral Fellow, Princeton University, USA
  • 1998  Postdoctoral fellow and staff scientist,  European Molecular Biology Laboratory, Germany
  • 2002  Team and group leader, European Molecular Biology Laboratory, Germany
  • 2011 Established lab at the London Research Institute, Cancer Research UK
  • 2015 Group Leader, the Francis Crick Institute, London, UK