Michael Way

Cellular Signalling and Cytoskeletal Function Laboratory.

The spatial and temporal control of cell adhesion and motility is essential during the development and throughout the lifetime of multi-cellular organisms. Unfortunately, deregulation of these two fundamental cellular processes frequently occurs during pathological situations such as tumour cell metastasis. Intracellular pathogens also frequently take advantage of the signaling networks and cytoskeleton of their hosts to facilitate their entry, replication, survival and spread.

Investigating exactly how pathogens hijack and subvert their unwilling hosts offers a unique opportunity to obtain mechanistic insights into the regulation and function of a multitude of cellular processes. To this end, we use a combination of quantitative imaging, genetic and biochemical approaches to study Vaccinia virus as a model system to interrogate the regulation and function of Src and Rho GTPase signalling networks, actin and microtubule-based transport as well as cell migration.

Outside the context of Vaccinia infection, we also investigate the cellular function of Tes, a tumour suppressor that negatively regulates Mena-dependent cell migration, Actin related proteins (Arps) as well as the mechanisms regulating the assembly and function of invadopodia.

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Figure

Figure. Viral plaque in a field of cultured cells

Selected publications

Chen XJ, Squarr AJ, Stephan R, Chen B, Higgins TE, Barry DJ, Martin MC, Rosen MK, Bogdan S, Way M. Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton. Developmental Cell 2014;30:569-584

Humphries AC, Donnelly SK, Way M. Cdc42 and the RhoGEF Intersectin-1 collaborate with Nck to promote N-WASP-dependent actin polymerization. Journal of Cell Science. 2014;127:673-685

Donnelly SK, Weisswange I, Zettl M, Way M. WIP provides an essential link between Nck and N-WASP during Arp2/3 dependent actin polymerization. Current Biology 2013;23:999-1006

Handa Y, Durkin CH, Dodding MP and Way M. Vaccinia Virus F11 promotes viral spread by acting as a PDZ-containing scaffolding protein to bind Myosin-9A and inhibit RhoA signaling. Cell Host and Microbe 2013;14:51-62

Humphries AC and Way, M. The non-canonical roles of clathrin and actin in pathogen internalization, egress and spread. Nature Reviews Microbiology 2013;11 551-560

Welch MD and Way M. Arp2/3-mediated actin-based motility: A tail of pathogen abuse. Cell Host and Microbe 2013;14:242-255

Humphries AC, Dodding MP, Barry DJ, Collinson LM, Durkin CH, Way M. Clathrin potentiates vaccinia-induced actin polymerization to facilitate viral spread. Cell Host and Microbe. 2012;12:346-359

Dodding MP and Way M. Coupling viruses to dynein and kinesin-1. EMBO J. 2011;30:3527-3539

Dodding MP, Mitter R, Humphries AC, Way M. A Kinesin-1 binding motif in vaccinia virus that is widespread throughout the human genome. EMBO J. 2011;30:4523-4538.

Weisswange I, Newsome TP, Schleich S, Way M. The rate of N-WASP exchange limits the extent of Arp2/3 complex dependent actin-based motility. Nature. 2009;458:87-91

Arakawa Y, Cordeiro JV, Schleich S, Newsome TP, Way M. The release of vaccinia virus from infected cells requires RhoA-mDia modulation of cortical actin. Cell Host and Microbe. 2007;1:227-240

Boëda B, Briggs DC, Higgins T, Garvalov BK, Fadden AJ, McDonald NQ, Way M. Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding. Molecular Cell. 2007;28:1071-1082

Valderrama F, Cordeiro JV, Schleich S, Frischknecht F, Way M. Vaccinia virus induced cell motility requires F11L-mediated inhibition of RhoA signalling. Science. 2006;311:377-381

Michael Way

michael.way@crick.ac.uk
+44 (0) 20 7269 3733

  • Qualifications and History
  • 1988 PhD in Structural Studies, Cambridge University, UK
  • 1989 Postdoctoral Fellow, LMB, Cambridge, UK
  • 1992 Postdoctoral Fellow, Whitehead Institute, Massachusetts, USA
  • 1995 Group Leader, Cell Biology Programme, EMBL, Germany
  • 2001 Established lab at the Imperial Cancer Research Fund, UK (in 2002 the Imperial Cancer Research Fund became Cancer Research UK)
  • 2015 Group Leader, the Francis Crick Institute, London, UK