Premium
Loss of histone deacetylase Hdac1 disrupts metabolic processes in intestinal epithelial cells
Author(s) -
Gonneaud Alexis,
Turgeon Naomie,
Boisvert François-Michel,
Boudreau François,
Asselin Claude
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.08.009
Subject(s) - hdac1 , histone deacetylase , microbiology and biotechnology , chemistry , histone , histone deacetylase 5 , hdac11 , histone deacetylase 2 , hdac10 , hdac4 , biochemistry , biology , gene
By using acetyl‐CoA as a substrate, acetyltransferases and histone deacetylases regulate protein acetylation by adding or removing an acetyl group on lysines. Nuclear‐located Hdac1 is a regulator of intestinal homeostasis. We have previously shown that Hdac1 define specific intestinal epithelial cell basal and inflammatory‐dependent gene expression patterns and control cell proliferation. We show here that Hdac1 depletion in cellulo leads to increased histone acetylation after metabolic stresses, and to metabolic disturbances resulting in impaired responses to oxidative stresses, AMPK kinase activation and mitochondrial biogenesis. Thus, nuclear Hdac1 may control intestinal epithelial cell metabolism by regulating the supply of acetyl groups.