Beyond the genome and proteome: targeting protein modifications in cancer

Nearly all proteins are modified in post translational events, indeed, understanding the control and function of post translational modifications (PTMs) is arguably the ‘next frontier’ for cancer cell biologists. The most well understood PTMs include glycosylation, phosphorylation, ubiquitination, methylation and palmitylation. Each of these modifications has been observed to be altered in cancer, affecting key cellular pathways including signal transduction, cell membrane receptor function, and protein–protein interactions. A number of strategies have been proposed that aim to target the modified proteins themselves, the enzymes that construct them, or that boost host-cellular immunity against modified residues aberrantly expressed in cancer.

► The majority of proteins are modified in post-translational events.
► Altered mucin glycosylation is characteristic of epithelial cancers.
► Current strategies aimed at harnessing PTM aberrations in cancer include histone protein deacetylase inhibitors.