英国莱斯特大学招聘分子医学博士后研究员

Open ended contract subject to funding. Funding available for 3 years

At Leicester we’re going places. Ranked in the top 20 universities in Britain our aim is to climb further. A commitment to high quality fused with an inclusive academic culture is our hallmark and led the Times Higher Education to describe us as “elite without being elitist”.

A postdoctoral research post is available within the research group of Richard Bayliss, Professor of Molecular Medicine in the Department of Biochemistry.

Chromosome segregation is effected by the mitotic spindle, a dynamic system of microtubules (MTs) and associated proteins that emanate from two poles that in adult human cells are formed around centrosomes. The mitotic spindle is the cellular target of two successful classes of cancer drug, the taxanes and vinca alkaloids, which interfere with MT function and therefore have dose-limiting side-effects on other tissues. Our studies on the mitotic spindle have the long-term aim of enabling the development of improved cancer drugs. To reach this point, we must first develop a comprehensive understanding of the molecular mechanisms that underpin mitotic spindle function.

K-fibres are bundles of microtubules that connect chromosomes to spindle poles. They are stabilized by a complex formed from three proteins: clathrin, TACC3 and ch-TOG. We have shown that clathrin and TACC3 together form a MT-binding module. The domains in clathrin and TACC3 that interact are adjacent to the domains that are required for MT binding, and the assembly of the complex is dependent on phosphorylation of TACC3 by Aurora-A kinase. The roles of ch-TOG in complex assembly and MT binding are unclear.

The overall aim of the project is to assemble a high-resolution model of the clathrin/TACC3/ch-TOG complex, capitalizing on our recent paper in which we identified the binding regions. We have two postdoctoral researchers funded on this project: the post in Prof. Bayliss’s group will focus on X-ray crystallography, protein-protein interaction studies and low-resolution methods such as SAXS and TIRF microscopy; a second postdoctoral researcher based in Dr Mark Pfuhl’s group in Kings College London will focus on NMR-based techniques. The two researchers will coordinate their efforts to piece the structures together into a model of the core MT-binding module of the complex. Our work will shed light on the regulation, assembly, dynamics and MT-binding properties of this complex.

Prof. Bayliss’s research group is located in the state-of-the-art Henry Wellcome Building with access to excellent facilities for biochemical studies, structural biology, cell culture, microscopy and computer analysis. The position is funded by the Biotechnology and Biological Sciences Research Council and is available from 1st September 2014 for three years. Prospective candidates should hold a degree and Ph.D in biochemistry, or related discipline, and have expertise in relevant structural biology and biophysical techniques.

Prof. Bayliss has an established track record in the study of microtubule binding proteins and their regulatory partners. The project builds on successful collaborations with Drs Stephen Royle and Anne Straube at the University of Warwick and Dr Mark Pfuhl at KCL.