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. 2022 Feb 8;5:114. doi: 10.1038/s42003-022-03060-1

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Ubiquitylation is an ATP-dependent process that depends on the cooperative action of three sequential enzymes: Ub-activating enzyme (E1), Ub-conjugating enzyme (E2), and Ub E3 ligase (E3). Ub (magenta) is attached covalently to a lysine (K) residue of a substrate protein (dark blue) either through direct transfer from the E2 enzyme to the substrate, or through sequential transfer from the E2 enzyme to the E3 ligase and then to the substrate. b Ubiquitin can form eight different linkage types, using one of seven internal lysine residues (K6, K11, K27, K29, K33, K48, K63) or methionine at position 1 (M1). Specific Ub chains are capable to confer distinct functions of targeted substrates and thereby regulate different cellular processes. The functions illustrated here for each given type of Ub-chain are not restricted to the biological pathway depicted, but are rather representative examples chosen for simplicit.