Justin Molloy

Single Molecule Enzymology Laboratory

The principal goal of the lab is to understand the molecular mechanism of force production by acto-myosin and how proteins and organelles move around within living cells. Laser-based optical methods like optical tweezers and total internal reflection fluorescence microscopy allow us to observe, track and manipulate individual molecules either in isolated preparations or within living cells.

Molecular motors convert chemical energy into mechanical work and power processes like muscle contraction, cell migration and DNA processing; they are critical to the healthy function of our cells. We are interested in diverse aspects of human health, including how the malarial parasite gains entry into human blood cells, the mechanism of human hearing, and how the two strands of DNA are separated and copied.

Our laser-based tools enable us to visualize and manipulate individual molecules so that we can understand molecular mechanisms with unprecedented precision. Recent work has shown how actin filaments become aligned by myosin motors in migrating cells, and dual-colour fluorescence imaging has allowed us to image individual G-protein coupled receptors at the cell membrane.

Figure 1

Optical tweezers (left) and Total Internal Reflection Fluorescence Microscopy (right) enable individual molecules to be manipulated and imaged. (Click to view larger image)

Selected publications

Takagi, Y; Farrow, RE; Billington, N; Nagy, A; Batters, C; Yang, Y; Sellers, JR and Molloy, JE (2014) Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load. Proceedings of the National Academy of Sciences of the United States of America 111, E1833-E1842

Hern, JA; Baig, AH; Mashanov, GI; Birdsall, B; Corrie, JET; Lazareno, S; Molloy, JE and Birdsall, NJM (2010) Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. Proceedings of the National Academy of Sciences of the United States of America 107, 2693-2698

Baboolal, TG; Sakamoto, T; Forgacs, E; White, HD; Jackson, SM; Takagi, Y; Farrow, RE; Molloy, JE; Knight, PJ; Sellers, JR and Peckham, M (2009) The SAH domain extends the functional length of the myosin lever. Proceedings of the National Academy of Sciences of the United States of America 106, 22193-22198

Justin Molloy

justin.molloy@crick.ac.uk
+44 (0)20 379 62352

  • Qualifications and History
  • BSc, Physiology, University of York, UK
  • PhD Biophysics, University of York, UK
  • 1995 - 2002 Royal Society University Research Fellow, York, UK
  • 2002 - Date Head of Division of Physical Biochemistry, Medical Research Council National Institute for Medical Research (MRC-NIMR), London, UK
  • 2005 - Date Head of Structural Biology Group, MRC-NIMR, London, UK
  • 2015 Group Leader, the Francis Crick Institute, London, UK