Ubiquitination is a post-translational modification that consists of ubiquitin attachment
to target proteins through sequential steps catalysed by activating (E1), conjugating
(E2), and ligase (E3) enzymes. Protein ubiquitination is crucial for the regulation of many
cellular processes not only by promoting proteasomal degradation of substrates but also
re-localisation of cellular factors and modulation of protein activity. Great importance
in orchestrating ubiquitination relies on E3 ligases as these proteins recognise the
substrate that needs to be modified at the right time and place. Here we focus
on two members of the TRIpartite Motif (TRIM) family of RING E3 ligases, MID1,
and MID2. We discuss the recent findings on these developmental disease-related
proteins analysing the link between their activity on essential factors and the regulation
of cytokinesis highlighting the possible consequence of alteration of this process in
pathological conditions.
