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. 2019 Jul 5;10:835. doi: 10.3389/fphys.2019.00835

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Copyright © 2019 Deol, Lorenz and Strieter.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The diversity of ubiquitin chains enables highly nuanced mechanisms of regulation. (A) Structure of ubiquitin (PDB: 1UBQ) showing the seven lysine side chains (K6, K11, K27, K29, K33, K48, and K63) and the N-terminus along with the I36 and I44-centered hydrophobic patches, highlighted in green (L8, I36, L70, and L73) and blue (L8, I44, H68, and V70), respectively. (B) Types of ubiquitin chains that can be produced. Homotypic chains are assembled using the same amino group of ubiquitin for each linkage, whereas heterotypic chains contain a mixture of linkages. Branched chains are a form of heterotypic chain, in which at least one ubiquitin molecule is modified by two or more ubiquitin molecules. (C) The relative orientation of the I36 and I44-centered hydrophobic patches controls how different chain types are recognized by effector proteins and DUBs.