Abstract
HECT ubiquitin ligases are key components of the eukaryotic ubiquitin-proteasome system controlling different cellular physiological aspects as well as the genesis of several human diseases. Among the HECT family, the HERC subfamily members are characterized by having one or more RCC1-like domains, a C-terminal HECT domain and the molecular mass ranging approximately from 120 kDa to 500 kDa. Due to their large size, some of them are refractory to functional characterization. We have recently identified and functionally characterized a novel large HECT member in Dictyostelium discoideum that, in many aspects, exhibits structural similarities with the mammalian large HERC1. In the present minireview, we shortly summarize and revise the current phylogenetic history of HERC proteins among the different living organisms.
Highlights
Ubiquitination, which is the covalent ligation of ubiquitin to a substrate protein, is associated with almost every cellular process including signal transduction, DNA damage repair, cell cycle regulation and autophagic clearance
We have recently identified and functionally characterized a novel large HECT member in Dictyostelium discoideum that, in many aspects, exhibits structural similarities with the mammalian large HERC1
In the present minireview, we shortly summarize and revise the current phylogenetic history of HERC proteins among the different living organisms
Summary
Ubiquitination, which is the covalent ligation of ubiquitin to a substrate protein, is associated with almost every cellular process including signal transduction, DNA damage repair, cell cycle regulation and autophagic clearance. E3 ligases carry out the final step in the ubiquitination cascade, catalysing the transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine[1] (Figure 1). In human beings RING is the largest family with more than 600 putative members that do not have a direct catalytic role in protein ubiquitination but basically, they act as scaffold facilitating the interaction between E2 and the substrates. In contrast to RING E3 ligases, the HECT and RBR family members catalyse the ubiquitin transfer to the substrate through a two-step reaction: ubiquitin is first transferred to a catalytic cysteine residue on the E3 and covalently linked to the substrate[3,4].
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