Ubiquitination is a post-translational modification (PTM) that is involved in proteolysis,
protein-
protein interaction, and signal transduction. Accumulation of mutations and
genomic instability are characteristic of
cancer cells, and dysfunction of the
ubiquitin pathway can contribute to abnormal cell physiology. Because mutations can be critical for cells, DNA damage repair, cell cycle regulation, and apoptosis are pathways that are in close communication to maintain genomic integrity. Uncontrolled cell proliferation due to abnormal processes is a hallmark of
cancer, and mutations, changes in expression levels, and other alterations of ubiquitination factors are often involved. Here, three E3
ubiquitin ligases will be reviewed in detail. RNF126, RNF168 and CUL1 are involved in DNA damage response (DDR),
DNA double-strand break (
DSB) repair, cell cycle regulation, and ultimately,
cancer cell proliferation control. Their involvement in multiple cellular pathways makes them an attractive candidate for
cancer-targeting
therapy. Functional studies of these E3
ligases have increased over the years, and their significance in
cancer is well reported. There are continuous efforts to develop drugs targeting the
ubiquitin pathway for anticancer
therapy, which opens up the possibility for these E3
ligases to be evaluated for their potential as a target
protein for anticancer
therapy.