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. 2021 Feb 4;12(2):154. doi: 10.1038/s41419-021-03441-0

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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. 1 — A Three catalytic subunits β1, β2, and β5 subunits can be replaced by their homologues β1i, β2i, and β5i to form immunoproteasome, β5t substitutes β5 to form thymoproteasome, and α4s subunits replace their constitutive counterparts α4 to form spermatoproteasome. B The combination of 20 S CP with proteasome activator. The 19 S or 11 S complex can associate at one or both ends of 20 S to form different types of proteasome.