| Literature DB >> 36098485 |
Natsuko Macabuag1, William Esmieu1, Perla Breccia1, Rebecca Jarvis1, Wesley Blackaby1, Ovadia Lazari1, Liudvikas Urbonas1, Maria Eznarriaga1, Rachel Williams1, Annelieke Strijbosch2, Rhea Van de Bospoort2, Kim Matthews1, Cole Clissold1, Tammy Ladduwahetty1, Huw Vater1, Patrick Heaphy3, Douglas G Stafford3, Hong-Jun Wang3, John E Mangette3, George McAllister4, Vahri Beaumont4, Thomas F Vogt4, Hilary A Wilkinson4, Elizabeth M Doherty4, Celia Dominguez4.
Abstract
Huntington's disease (HD) is a lethal autosomal dominant neurodegenerative disorder resulting from a CAG repeat expansion in the huntingtin (HTT) gene. The product of translation of this gene is a highly aggregation-prone protein containing a polyglutamine tract >35 repeats (mHTT) that has been shown to colocalize with histone deacetylase 4 (HDAC4) in cytoplasmic inclusions in HD mouse models. Genetic reduction of HDAC4 in an HD mouse model resulted in delayed aggregation of mHTT, along with amelioration of neurological phenotypes and extended lifespan. To further investigate the role of HDAC4 in cellular models of HD, we have developed bifunctional degraders of the protein and report the first potent and selective degraders of HDAC4 that show an effect in multiple cell lines, including HD mouse model-derived cortical neurons. These degraders act via the ubiquitin-proteasomal pathway and selectively degrade HDAC4 over other class IIa HDAC isoforms (HDAC5, HDAC7, and HDAC9).Entities:
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Year: 2022 PMID: 36098485 PMCID: PMC9512014 DOI: 10.1021/acs.jmedchem.2c01149
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 8.039