Casein Kinase-2α1 Induces Hypertrophic Response by Phosphorylation of Histone Deacetylase 2 S394 and its Activation in the Heart
Author(s) -
Gwang Hyeon Eom,
Young Kuk Cho,
JeongHyeon Ko,
Sera Shin,
Nakwon Choe,
Yoojung Kim,
Hosouk Joung,
Hyung-Seok Kim,
Kwang Il Nam,
Hae Jin Kee,
Hyun Kook
Publication year - 2011
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.110.003665
Subject(s) - histone deacetylase 2 , muscle hypertrophy , phosphorylation , trichostatin a , medicine , endocrinology , casein kinase 2 , transgene , kinase , histone deacetylase , biology , protein kinase a , histone , microbiology and biotechnology , biochemistry , mitogen activated protein kinase kinase , gene
Cardiac hypertrophy is characterized by transcriptional reprogramming of fetal gene expression, and histone deacetylases (HDACs) are tightly linked to the regulation of those genes. We previously demonstrated that activation of HDAC2, 1 of the class I HDACs, mediates hypertrophy. Here, we show that casein kinase-2α1 (CK2α1)-dependent phosphorylation of HDAC2 S394 is required for the development of cardiac hypertrophy.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom