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Cells 2014, 3(3), 674-689;

Mechanisms of Generating Polyubiquitin Chains of Different Topology

CSIRO Materials Science and Engineering, Parkville, Victoria 3052, Australia
Cell Cycle and Cancer Unit, St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia
Department of Medicine, St. Vincent's Hospital, University of Melbourne, Fitzroy, Victoria 3065, Australia
Author to whom correspondence should be addressed.
Received: 13 May 2014 / Revised: 11 June 2014 / Accepted: 19 June 2014 / Published: 1 July 2014
(This article belongs to the Special Issue Protein Ubiquitination)
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Ubiquitination 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. View Full-Text
Keywords: protein ubiquitination; ubiquitin chain topologies; polyubiquitination protein ubiquitination; ubiquitin chain topologies; polyubiquitination

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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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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.

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