Functional Roles of Ubiquitin-Like Domain (ULD) and Ubiquitin-Binding Domain (UBD) Containing Proteins

The ubiquitin landscape at DNA double-strand breaks

“…Consistent with the structural diversity of ubiquitin chains, a myriad of ubiquitin-binding domains exists that recognizes different features and topologies of ubiquitin. The majority of ubiquitinbinding domains form -helical structures that recognize the hydrophobic patch centered around Ile44 of ubiquitin (Harper and Schulman, 2006;Grabbe and Dikic, 2009). Though the affinities of individually isolated ubiquitin-binding domains are low to moderate, this affinity may increase in vivo due to multiple ubiquitin-binding members in a complex recognizing polyubiquitin chains in a synergistic fashion.…”

A distinct structural region of the prokaryotic ubiquitin‐like protein (Pup) is recognized by the N‐terminal domain of the proteasomal ATPase Mpa

“…The recognition of polyubiquitinated substrates at the eukaryotic 19S regulatory particle involves ubiquitin receptors featuring ubiquitin-binding domains [17]. Analogously, the suggested ATPase partner of the mycobacterial proteasome, Mpa (referred to as ARC in other actinobacteria), was shown to interact with Pup [14,15].…”

Protein Phosphorylation in Human Health

“…Whereas poly-ubiquitination linked to K48 residues is usually related to proteasomal degradation [158], K63-linked polyubiquitin chains are more related to other regulatory functions [159]. In addition to the conjugating lysine, ubiquitin chains display an ample structural diversity, that has its counterpart in many different ubiquitin interactif motifs (UIM) in other proteins [160]. The role of UQ is counteracted by deubiquitianting enzymes (DUB), which are responsible for the elimination of UQ conjugates.…”