Yeast organellar transport
- Transport across the nuclear pore complex
- Vacuolar transport
Transport across the nuclear pore complex (Prof. Dr. B. Poolman, Dr. L.M. Veenhoff)
A multitude of proteins and messenger ribonucleoproteins (mRNPs) translocate between the nucleus and the cytoplasm through the ~ 50 MDa nuclear pore complex (NPC1,2). Molecules smaller than ~ 5 nm in diameter can diffuse freely through these pores, whereas larger molecules are selectively imported into or exported from the nucleus by facilitated diffusion. The nucleocytoplasmic transport generally starts with the binding of a member of the β-karyopherin superfamily to the nuclear localization signal (NLS) of the cargo molecule. The karyopherin-cargo complex can translocate through the NPC, and the cargo is released on the other side of the membrane via interactions with RanGTP. We have developed a method to monitor transport of cargo through the NPC, using selective-FRAP, in situ. Within this project, the translocation properties of the NPC and protein composition (and functions) of the nuclear envelope are determined.
- Alber, F., Dokudovskaya, S., Veenhoff, L.M. et al. (2007) The molecular architecture of the nuclear pore complex. Nature, 450, 695-701.
- Alber, F., Dokudovskaya, S., Veenhoff, L.M. et al. (2007) Determining the architectures of macromolecular assemblies by integrating spatial restraints from proteomic data. Nature, 450, 683-694 .
Vacuolar transport (Prof. Dr. B. Poolman, Prof. Dr. D.J. Slotboom)
We study secondary active transporters involved transport of solutes between the cytoplasm and the vacuolar lumen in Saccharomyces cerevisiae.
Wiederhold, E., Gandhi, T., Permentier, H.P., Breitling, R., Poolman, B., and Slotboom, D.J.
The yeast vacuolar membrane proteome. Mol Cell Proteomics. 2009; 8(2):380-92.
|Last modified:||03 October 2012 12.04 p.m.|