The Selectivity of the Nuclear Pore Complex

Proteins required in the nucleus of the cell are initially synthesized in the cytoplasm, and must then be transported across the nuclear membrane to reach their destination. Similarly, the mRNA from which proteins are translated has to be transported from the nucleus to the cytoplasm. In both cases, these macromolecules are transported across the nuclear envelope through nuclear pore complexes, cylindrical proteinaceous structures about 120nm in diameter and 70nm thick that perforate the nuclear membrane.

This project will focus on the question: How does the nuclear pore select only those proteins meant for the nucleus, while blocking other (often much smaller) proteins from entering? In particular, we will be explore the role played by long disordered proteins that are located in the pore and have binding sites for carrier proteins, which form complexes with the biomolecules that need to be transported across the pore. The project will involve simulations at a variety of levels of detail to probe the physical mechanism by which these "polymers" mediate this selectivity.

This project is in collaboration with the group of Dr Ard Louis in The Rudolf Peierls Centre for Theoretical Physics and Dr Murray Stewart of the MRC Laboratory for Molecular Biology in Cambridge.