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. 2021 Dec 2;9:719390. doi: 10.3389/fcell.2021.719390

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Copyright © 2021 Zhou, Liu and Tan.

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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Structure of HDAC6 protein. The HDAC6 protein contains two functional catalytic domains (CD) that catalyze deacetylation. The nuclear export signal (NES) helps cytoplasmic localization, and the Ser-Clu–containing tetrapeptide (SE14) is responsible for the stable anchorage of the enzyme in the cytoplasm. Its nuclear localization sequence (NLS) mainly locates in the cytoplasm due to the interaction of NES and SE14 motifs. In the C-terminal region of the protein, the ubiquitin-binding zinc finger domain (UBP) constitutes a high-affinity ubiquitin-binding motif.