; University of Glasgow
The Fanconi Anemia DNA repair pathway is needed to fix DNA interstrand crosslinks. At the heart of the pathway is a single monoubiquitin signal which is attached to two homologous proteins, FANCD2 and FANCI. Both the assembly and the removal of the signal are required for completion of interstrand crosslink repair. My lab focusses on understanding the mechanisms of assembly, functional consequence, and removal of specific ubiquitin signals. I will present our biochemical and structural data defining each of these steps, from how a single site is targeted for modification, what the addition of ubiquitin does to the ID2 complex, how each ubiquitin signal has a distinct function, and how the signal is removed from a specific site.
Current role: Head of School of Molecular Biosciences at the University of Glasgow
BSc in Biochemistry from the University of Bath in 1998
PhD in Structural Biology from the University of St Andrews, 2001
Postdoc at St Jude Children鈥檚 research hospital 2001-2005 in Brenda Schulman鈥檚 lab
2005 - 2013 Group leader at the London Research Institute of Cancer Research UK (now the Francis Crick Institute)
2013-2017 Professor of structural biology at the University of Dundee
2017 - now Professor of structural biology at the University of Glasgow
Other notable things:
EMBO Young Investigator 2012-2014
Colworth Medal of Biochemical Society 2015
Fellow of Royal Society of Edinburgh 2022
EMBO member 2022
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