Dr James Sullivan
Lecturer
- Room: 4.34, Fogg building
- Telephone: +44 (0)20 7882 6360
- Email: j.a.sullivan("at" sign)qmul.ac.uk
Research interests:
The degradation of proteins is an essential process for cell survival, both for quality control of damaged or misfolded proteins and for the down-regulation of unwanted and/or activated receptors or transporters. Ubiquitin is a highly conserved 8 kDa protein, which can be covalently linked to lysine residues in proteins. Ubiquitination is one of the most important post-translational modifications that takes place within the eukaryotic cell. The addition of single or multiple ubiquitin moieties to a target protein can lead to different fates, from degradation following polyubiquitination to endocytosis from the plasma membrane following monoubiquitination. Ubiquitin has been implicated in a huge range of developmental processes and this is reflected in the large number of diseases in which aberrant ubiquitination is a feature. Central to the process of ubiquitination and therefore the fate of the substrate are a group of proteins known as ubiquitin ligases, which, by binding to the target protein, control specificity.
Research in my group focuses on understanding how ubiquitin ligases recognize their substrates and how these processes are controlled. Current research involves the use of genetic and biochemical techniques in yeast and in human tissue culture cells to investigate the highly conserved Nedd4-family of ubiquitin ligases.
Research group:
Postgraduate supervision:
Marks, Helen; h.marks ("at" sign) qmul.ac.uk;