The Department of Pathology is one of the largest Departments in the School of Biological Sciences, and a leading research institution with a yearly research income of £9M. The Department's research seeks to understand - and so ultimately arrest and reverse - disease processes of medical and social significance. The work of the Department is organised into five Divisions: Cell and Molecular Pathology, Immunology, Microbiology and Parasitology, Virology and Molecular Histopathology, split between the University site and Addenbrooke's Hospital, as well as undertaking cross-disciplinary research with colleagues at Research Institutes including the Cambridge Institute for Medical Research and the Hutchison-MRC Institute for Cancer Research.
The Department also has a major yearly commitment in the teaching and training to over 800 undergraduate students of medicine and of veterinary and natural science. In its research laboratories it provides training for over 70 graduate students. Members of the Department also contribute, together with colleagues in the National Health Service and Health Protection Agency, to provision of diagnostic services within Addenbrooke's Hospital and the Anglia Region.
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- Jeffrey Pollard, University of Edinburgh and Albert Einstein College of Medicine, New York
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The surface of the cell is a highly dynamic membrane that is constantly remodelled as cells take up nutrients and respond to signals from their environment. The AP2 protein complex regulates this remodelling by recognising which ‘cargo’ molecules on the cell surface should be taken up. Upon binding to cargo AP2 recruits clathrin, a scaffold protein required for deforming the cell’s surface, to form buds that deliver the cargo to the interior of the cell. In a paper recently published in Science, Stephen Graham collaborated with groups in the Cambridge Institute for Medical Research and in Germany to show how AP2 prevents clathrin recruitment until it has sensed a cargo molecule on the cell surface. It does this by hiding its clathrin-binding signal peptide in a deep pocket on its surface. Upon sensing cargo at the cell surface the AP2 complex undergoes a dramatic reorganisation that closes the pocket and forces the clathrin recruitment signal to spring free. Thus liberated, the signal peptide can bind clathrin to promote deformation of the cell surface and movement of molecules into the cell.
B.T. Kelly, S.C. Graham, N. Liska, P.N. Dannhauser, S. Höning, E.J. Ungewickell, D.J. Owen (2014) AP2 controls clathrin polymerization with a membrane-activated switch. Science, 345: 459–463. DOI: 10.1126/science.1254836