Histone Deacetylase 1-Mediated Histone Modification Regulates Osteoblast Differentiation
نویسندگان
چکیده
منابع مشابه
A Histone Deacetylase Regulates Addiction
Epigenetic modification of chromatin has been proposed to translate environmental stimuli into persistent "cellular memories." Recent studies suggest that epigenetic pathways regulate long-term behavioral adaptation in the nervous system. In this issue of Neuron, Renthal et al. utilize genetic manipulations of HDAC5 to provide strong evidence for a role for histone acetylation in the behavioral...
متن کاملHistone deacetylase 6 regulates human immunodeficiency virus type 1 infection.
Efficient human immunodeficiency virus (HIV)-1 infection depends on multiple interactions between the viral gp41/gp120 envelope (Env) proteins and cell surface receptors. However, cytoskeleton-associated proteins that modify membrane dynamics may also regulate the formation of the HIV-mediated fusion pore and hence viral infection. Because the effects of HDAC6-tubulin deacetylase on cortical al...
متن کاملHistone deacetylase 1 regulates tissue destruction in rheumatoid arthritis.
Emerging evidence implicates epigenetic mechanisms in the pathogenesis of rheumatoid arthritis (RA). In this study, we have investigated the role of histone deacetylase (HDAC) enzymes in RA synovial fibroblasts (RASFs), a key cellular mediator of cartilage and bone destruction and determined effects of HDAC1 inhibition on both RASF phenotype in vitro, and joint inflammation and damage in the co...
متن کاملSumoylation of histone deacetylase 1 regulates MyoD signaling during myogenesis
Sumoylation, the conjugation of a small ubiquitin-like modifier (SUMO) protein to a target, has diverse cellular effects. However, the functional roles of the SUMO modification during myogenesis have not been fully elucidated. Here, we report that basal sumoylation of histone deacetylase 1 (HDAC1) enhances the deacetylation of MyoD in undifferentiated myoblasts, whereas further sumoylation of H...
متن کاملHistone deacetylase 3 regulates cyclin A stability.
PCAF and GCN5 acetylate cyclin A at specific lysine residues targeting it for degradation at mitosis. We report here that histone deacetylase 3 (HDAC3) directly interacts with and deacetylates cyclin A. HDAC3 interacts with a domain included in the first 171 aa of cyclin A, a region involved in the regulation of its stability. In cells, overexpression of HDAC3 reduced cyclin A acetylation where...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular Endocrinology
سال: 2006
ISSN: 0888-8809,1944-9917
DOI: 10.1210/me.2006-0061