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. 2021 Jan 26;7:6. doi: 10.1038/s41421-020-00237-y

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© The Author(s) 2021

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. 2 — The APC/C collaborates with two different E2s, UBE2C and UBE2S, to assemble branched K11/K48 chains on cyclin A and other mitotic substrates. UBR5 collaborates with an unknown K11-specific E3 to form branched K11/K48 chains of a different architecture on a pathological mutant version of the Huntingtin protein (HTT-Q73). UBR5 has also been reported to synthesize branched K11/K48 chains on newly synthesized misfolded polypeptides¹¹. Spt23 and substrates of the ubiquitin fusion degradation pathway are modified with branched K29/K48 chains synthesized by Ufd4 and Ufd2. ITCH cooperates with UBR5 to assemble branched K48/K63 chains on the pro-apoptotic regulator TXNIP. Substrates are colored in green; chain branching E3s are colored in light blue; the color coding for ubiquitins is as described in Fig. 1.