Robert Cross

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ResearcherID: F-1798-2011

ResearcherID (2013-03-10)


I obtained my PhD from Nottingham University in 1983 and then won an EMBO fellowship to work with Vic Small and Apolinary Sobieszek in Salzburg on the structure and mechanisms of smooth muscle. I discovered that a C-terminal sequence of myosin II is essential for its self-assembly and that the self-assembly of myosin II molecules is dynamically controlled via nucleotide trapping in their active sites. In 1986 I won an MDA fellowship to work at MRC-LMB in Cambridge with John Kendrick Jones. With Jake, Clive Bagshaw and Mike Geeves, I worked out an explicit mechanism for myosin II self-assembly. In 1991 I moved to start my own lab at Marie Curie Cancer Research. With Linda Amos and Keiko Hirose at LMB, we obtained the first EM views of microtubule-bound kinesin (Nature, 1995). Subsequently, we discovered that at high load, kinesins can walk processively backwards (Nature, 2005), that ATP binding gates their ability to bind tubulin (Science, 2007), that their force generation mechanism generates torque (Nature Chemical Biology, 2005) and that kinesins can sort and parallelise microtubules (Nature Cell Biology, 2009). In 2010, I moved to Warwick University, to co-found the CMCB, a new interdisciplinary centre for mechanochemical cell biology. At Warwick we have shown that kinesin motors are electrostatically steered (PLOS Biology, 2011), that microtubule seams are hotspots of instability (Nature Communications, 2014), that kinesin can be programmed using DNA (Nature Nanotechnology, 2015) and that yeast kinesin-5 reverses its stepping direction using a proximity sensing mechanism (PNAS, 2016). Most recently, we have shown that kinesin binding radically changes the conformation and mechanics of GDP-microtubules ( I am a Wellcome Senior Investigator and a member of the Wellcome Expert Review Group in the Molecular Basis of Cell Function.

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