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Mechanisms of Generating Polyubiquitin Chains of Different Topology
AbstractUbiquitination is an important post-translational process involving attachment of the ubiquitin molecule to lysine residue/s on a substrate protein or on another ubiquitin molecule, leading to the formation of protein mono-, multi- or polyubiquitination. Protein ubiquitination requires a cascade of three enzymes, where the interplay between different ubiquitin-conjugating and ubiquitin-ligase enzymes generates diverse ubiquitinated proteins topologies. Structurally diverse ubiquitin conjugates are recognized by specific proteins with ubiquitin-binding domains (UBDs) to target the substrate proteins of different pathways. The mechanism/s for generating the different ubiquitinated proteins topologies is not well understood. Here, we will discuss our current understanding of the mechanisms underpinning the generation of mono- or polyubiquitinated substrates. In addition, we will discuss how linkage-specific polyubiquitin chains through lysines-11, -48 or -63 are formed to target proteins to different fates by binding specific UBD proteins.
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Suryadinata, R.; Roesley, S.N.A.; Yang, G.; Šarčević, B. Mechanisms of Generating Polyubiquitin Chains of Different Topology. Cells 2014, 3, 674-689.View more citation formats
Suryadinata R, Roesley SNA, Yang G, Šarčević B. Mechanisms of Generating Polyubiquitin Chains of Different Topology. Cells. 2014; 3(3):674-689.Chicago/Turabian Style
Suryadinata, Randy; Roesley, Siti N.A.; Yang, George; Šarčević, Boris. 2014. "Mechanisms of Generating Polyubiquitin Chains of Different Topology." Cells 3, no. 3: 674-689.