Dr Edward Morris
Division of Structural Biology
Tel: 020 7153 5531
Email: edward.morris@icr.ac.uk
Location: Chester Beatty Laboratories, London
Research Summary
The Structural Electron Microscopy TeamĀ
Fundamental cellular functions and cell division are regulated by large protein complexes. The pathways regulated by such complexes are often deregulated in cancer and they are targets for the development of anticancer drugs. It is therefore of great importance to fully understand the organisation and mechanism of such protein assemblies.
The Structural Electron Microscopy Team focuses on the use of electron microscopy and image analysis based methods to determine the three-dimensional structure and explain the function of large multi protein complexes. At the moment, our main project areas involve research into the structure of the 26S proteasome and the COP9 signalosome, components of the ubiquitin-proteasome system which plays a vital role in the regulation of cell division and cellular homeostasis.
We also take part in collaborative research with other groups both within and outside the Institute of Cancer Research.
Biography
Dr Edward Morris studied for his BA in Biochemistry at Cambridge and for his PhD in Biophysics at Kings College, London. After working as a postdoctoral fellow at Boston Biomedical Research Institute, Boston USA, Kings College London and Imperial College London, he set up his own laboratory in the Faculty of Medicine at Imperial College. In 2005, he moved to the Division of Structural Biology at The Institute of Cancer Research to set up a new laboratory specialising in structural analysis of protein complexes by electron microscopy-based methods. His main, current research projects focus on the structural analysis of protein complexes of the ubiquitin-proteasome system, which is involved in cellular regulation.
Structural Electron Microscopy
Structural Electron Microscopy is a technique which is particularly effective in determining the three-dimensional structure of large protein complexes.
26S proteasome
Selective protein removal is an essential regulatory mechanism in cellular homeostasis and cell division. The ubiquitin-proteasome system is responsible for the highly regulated targeting and proteolysis of such proteins. The 26S proteasome is a key component of the ubiquitin-proteasome system.
