Chromosomes; Nuclear Envelope; Nuclear Pore Complex Proteins
Discovery to Cure Internship
The Lusk lab focuses on understanding the molecular mechanisms that control the organization, structure and function of the nuclear envelope: the membrane system that encapsulates the genome of all eukaryotes.
At the heart of this pursuit is the examination of the function of membrane proteins that selectively enrich at the nuclear envelope. Mutation or deletion of several genes encoding these proteins have profound effects on cellular processes that result in the loss of nuclear envelope structure along with changes in gene expression and an increase in genome instability. These phenotypes often lead to cell death or the manifestation of specific diseases termed nuclear envelopathies. To fully understand the mechanisms that contribute to these essential processes, we have identified conserved integral membrane proteins in the budding yeast S. cerevisiae. Using yeast as a model system allows us to use a myriad of genetic, biochemical and cell biological methodology to directly examine how membrane proteins affect various aspects of nuclear envelope physiology. Ongoing projects in the lab include (a) defining mechanisms of nuclear pore complex assembly and distribution (b) understanding membrane protein traffic to the inner nuclear membrane (c) investigating the role of membrane proteins in controlling transcription, gene recruitment and genome stability at the nuclear periphery.
- Webster, BM, Colombi, P, Jager, J, Lusk, CP. Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4. Cell. 2014. 159(2): 388-401
- Colombi, P, Webster, BM, Frohlich, F, Lusk, C.P. The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1. Journal of Cell Biology. 2013. 203(2)
- Yewdell, W.T., Colombi, P, Makhnevych, T., Lusk C.P. Lumenal interactions in nuclear pore complex assembly and stability. Molecular Biology of the Cell. 2011. 22(8):1375-88
- Lusk, C.P., Blobel, G., King M.C. Highway to the inner nuclear membrane: rules for the road. Nature Reviews Molecular and Cellular Biology. 2007, 8: 414-420.
- King, M.C.*, Lusk C.P.*, G. Blobel. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature. 2006, 442: 1003-7 * equal contributions
- Lusk, C.P., T. Makhnevych, M. Marelli, J.D. Aitchison, R.W. Wozniak. Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes. Journal of Cell Biology. 2002, 159: 267-278.