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Updated: Jul 15, 2026
08:34
Mechanism of Regulation of Adipocyte Numbers in Adult Organisms Through Differentiation and Apoptosis Homeostasis
Published on: June 3, 2016
JDP2 suppresses adipocyte differentiation by regulating histone acetylation
1Gene Engineering Division, RIKEN, 3-1-1 Koyadai, Tsukuba Science City, Ibaraki 305-0074, Japan.
Cell Death and Differentiation
|April 28, 2007
Summary
Jun dimerization protein 2 (JDP2) represses adipocyte differentiation by inhibiting histone acetylation. Loss of JDP2 in mice leads to increased white adipocytes and lipid accumulation, highlighting JDP2
Area of Science:
- Molecular Biology
- Cell Biology
- Epigenetics
Background:
- Histone acetylation is crucial for regulating gene transcription and chromatin structure during cellular differentiation.
- Jun dimerization protein 2 (JDP2), an AP-1 family member, acts as an inhibitor of histone acetylation, maintaining chromatin structure.
Purpose of the Study:
- To investigate the role of JDP2 in adipocyte differentiation.
- To elucidate the mechanism by which JDP2 regulates adipogenesis.
Main Methods:
- Utilized Jdp2 knock-out (KO) mice and their derived mouse embryo fibroblasts (MEFs).
- Analyzed adipocyte differentiation, lipid accumulation, and gene expression (CCAAT/enhancer-binding proteins - C/EBP).
- Assessed histone H3 acetylation and gene transcription at the C/EBPdelta promoter.
Main Results:
- Jdp2 KO mice exhibited increased white adipocyte numbers and lipid accumulation in adipose tissue.
- MEFs from Jdp2 KO mice showed enhanced susceptibility to adipocyte differentiation.
- JDP2 was found to inhibit histone H3 acetylation and transcription of the C/EBPdelta gene.
Conclusions:
- JDP2 functions as a key repressor of adipocyte differentiation.
- JDP2 regulates C/EBPdelta gene expression through the inhibition of histone acetylation.
- These findings provide insights into the epigenetic regulation of adipogenesis.
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