2016
DOI: 10.1038/cr.2016.39
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Ubiquitin modifications

Abstract: Protein ubiquitination is a dynamic multifaceted post-translational modification involved in nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid protein ubiquitin is subjected to further modifications, creating a multitude of distinct signals with distinct cellular outcomes, referred to as the 'ubiquitin code'. Ubiquitin can be ubiquitinated on seven lysine (Lys) residues or on the N-terminus, leading to polyubiquitin chains that can encompass complex topologies. Alternati… Show more

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Cited by 1,582 publications
(1,471 citation statements)
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References 204 publications
(356 reference statements)
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“…All these chains vary in length, ranging from two to more than ten residues. They can be homotypic if the same residue is modified during elongation as in M1, K11, 48 or 63-linked chains, or heterotypic if the same chain displays different linkages [21,22]. Moreover, a single ubiquitin can be modified with multiple chains or UBLs (NEDD8, SUMO, ISG15), generating branched chains or mixed chains, respectively.…”
Section: Ubiquitination and Ubiquitin-like Modifiers (Ubls)mentioning
confidence: 99%
See 1 more Smart Citation
“…All these chains vary in length, ranging from two to more than ten residues. They can be homotypic if the same residue is modified during elongation as in M1, K11, 48 or 63-linked chains, or heterotypic if the same chain displays different linkages [21,22]. Moreover, a single ubiquitin can be modified with multiple chains or UBLs (NEDD8, SUMO, ISG15), generating branched chains or mixed chains, respectively.…”
Section: Ubiquitination and Ubiquitin-like Modifiers (Ubls)mentioning
confidence: 99%
“…Moreover, a single ubiquitin can be modified with multiple chains or UBLs (NEDD8, SUMO, ISG15), generating branched chains or mixed chains, respectively. Finally, ubiquitin can be acetylated or phosphorylated [21][22][23][24][25]. K48-linked ubiquitin was the first described poly-ubiquitin chain related to degradation [21,26].…”
Section: Ubiquitination and Ubiquitin-like Modifiers (Ubls)mentioning
confidence: 99%
“…This type of ubiquitination contributes to the recognition of signals for the ATP‐dependent breakdown of substrate proteins by the 26S proteasome pathway. In polyubiquitination, a chain of Ub molecules is attached to a single Lys residue in the target protein, which mainly takes part in the proteasomal degradation, protein trafficking, spindle assembly during cell cycle and DNA repair3 (Figure 1C). In particular, the misfolded proteins are removed by the Ub‐proteasome system to maintain the cellular environment and biological events such as cellular proliferation, apoptosis and survival.…”
Section: Ubiquitin Modificationsmentioning
confidence: 99%
“…Then, the activated Ub is transferred to the cysteine residue in the active site of E2. In the final step, E3 ligase is involved in the transfer of Ub from the E2 to a specific lysine residue of the substrate protein2, 3 (Figure 1B). As for phosphorylation, ubiquitination is a reversible process in which the attached Ub is removed from the target proteins by deubiquitylation enzymes (DUBs; Figure 1B).…”
Section: Introductionmentioning
confidence: 99%
“…Cell Research (2017) [3] was published in the April issue of 2016, as part of a special issue on ubiquitin and ubiquitin-like protein (Ubl) signaling [4] featuring a collection of seven authoritative reviews from worldwide renowned experts in the field. This review presents an overview of several types of ubiquitin-protein modifications in cells and the distinct roles of specific polyUb chains in cellular signaling.…”
Section: Sanofi-cell Research Outstanding Paper Award Of 2016mentioning
confidence: 99%