A novel proteomics approach could help scientists to identify the protein component of cell organelles, even in impure samples.

In eukaryotic cells, clathrin-coated vesicles (CCVs) are vital for transporting protein cargo from one part of the cell to another. Originally, scientists thought that clathrin and so-called 'adaptor proteins' were sufficient to make CCVs, but research has shown that these vesicles contain many additional proteins. While scientists can identify CCV proteins present in cells, it is unclear which are genuine components and which are contaminants, because completely pure CCVs cannot be made in the lab.

Margaret Robinson, Georg Borner and colleagues at the University of Cambridge have used an elegant but simple comparative proteomics solution to weed out the contaminants.

In all, the team identified 63 CCV proteins, almost half of which have not been associated with CCVs previously. The researchers believe that this comparative proteomics approach will be valuable in unpicking the protein composition of other organelles.

Above image: Comparative proteomic analysis of clathrin-coated vesicles. From Bourner et al.

External link

• Borner GH et al. Comparative proteomics of clathrin-coated vesicles. J Cell Biol 2006;175(4):571–8.