Membrane protein sorting
Equally important for the cell is the ability to remove unwanted or damaged proteins. Misfolded proteins are frequently degraded in the endoplasmic reticulum, but once proteins leave the ER the main route to destruction is via the multivesicular body pathway to lysosomes or vacuoles. This is the fate of proteins whose degradation is regulated - such as activated signalling receptors, or excess transporters and channels. These proteins are marked for degradation by addition of the small protein ubiquitin to their cytoplasmic domains, the attached tag acting as a sorting signal for the multivesicular body pathway.
We are currently studying the mechanisms by which proteins are modified and sorted, and seeking novel inhibitors of these processes.
- Mund, T. and Pelham, H.R.B. (2010)
Regulation of PTEN/Akt and MAP kinase signalling pathways by the ubiquitin ligase activators Nfip1 and Ndfip2.
Proc Natl Acad Sci USA 107: 11429-11434.
- Mund, T. and Pelham, H.R.B. (2009)
Control of the activity of WW-HECT domain E3 ubiquitin ligases by Ndfip proteins.
EMBO Rep 10: 501-507.
- Nikko, E. and Pelham, H.R.B. (2009)
Arrestin-mediated endocytosis of yeast plasma membrane transporters.
Traffic 10: 1856-1867.
- Michael Lewis
- Thomas Mund
- Elise Bernard