Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors

Chiara Lambona; Clemens Zwergel; Rossella Fioravanti; Sergio Valente; Antonello Mai

doi:10.1016/j.sbi.2023.102668

Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors

Curr Opin Struct Biol. 2023 Oct:82:102668. doi: 10.1016/j.sbi.2023.102668. Epub 2023 Aug 4.

Authors

Chiara Lambona¹, Clemens Zwergel¹, Rossella Fioravanti², Sergio Valente¹, Antonello Mai³

Affiliations

¹ Department of Drug Chemistry and Technologies, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.
² Department of Drug Chemistry and Technologies, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy. Electronic address: rossella.fioravanti@uniroma1.it.
³ Department of Drug Chemistry and Technologies, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy; Pasteur Institute, Sapienza University of Rome, Piazzale Aldo Moro 5, 00185 Rome, Italy.

PMID: 37542907
DOI: 10.1016/j.sbi.2023.102668

Abstract

Polyamine deacetylase activity was discovered more than 40 years ago, but the responsible histone deacetylase 10 (HDAC10) was described only recently. HDAC10 is a class IIb HDAC, as is its closest relative, the α-tubulin deacetylase HDAC6. HDAC10 has attracted attention over the last 2 years due to its role in diseases, especially cancer. This review summarises chemical and structural biology approaches to the study of HDAC10. Light will be shed on recent advances in understanding the complex structural biology of HDAC10 and the discovery of the first highly selective HDAC10 inhibitors.

Keywords: Crystallography; HDAC10; HDAC10 inhibitors; HDAC10 substrates; Polyamine deacetylase.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Catalytic Domain
Histone Deacetylases* / chemistry
Polyamines*

Substances

Polyamines
Histone Deacetylases