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Title 

Dephosphorylation of CCAAT/enhancer-binding protein β by protein phosphatase 2A containing B56δ is required at the early time of adipogenesis

Authors 

M ParkY A ChoiHee Gu LeeK I KimJ S LimM S LeeK S OhY Yang

Publisher 

Elsevier

Issue Date 

2014

Citation 

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, vol. 1841, no. 11, pp. 1608-1618

Keywords 

AdipogenesisB56δC/EBPβExtracellular signal regulated kinase (ERK)Protein phosphatase 2A (PP2A)

Abstract 

It is known that protein phosphatase 2A (PP2A) expression is increased in high-fat diet (HFD)-induced obese mice, but the role of PP2A in adipogenesis as well as obesity remains to be addressed. In this study, the role of PP2A in adipogenesis was explored. Preadipocytes were treated with okadaic acid (OA) during adipogenesis and the degree of adipogenesis was determined. The OA treatment blocked adipogenesis at the early time of adipogenesis, but not at the late time. In the early time of adipogenesis, CCAAT/enhancer-binding protein β (C/EBPβ) activation is preceded by the expression of key adipogenic transcription factors including PPARγ and C/EBPα, which function at the late time of adipogenesis, and then C/EBPβ is degraded. However, the inhibition of PP2A by OA treatment sustained phosphorylation of C/EBPβ and delayed its degradation. In turn, PPARγ and C/EBPα activation was altered. Among the various regulatory B56 subunits consisting of PP2A holoenzyme, B56δ was directly bound to C/EBPβ and was responsible for the dephosphorylation of C/EBPβ by PP2A. Taken together, these findings suggest that the phosphorylation of C/EBPβ after hormonal induction has to be inactivated by PP2A containing B56δ at the early time of adipogenesis to allow the completion of adipogenesis.

ISSN 

1388-1981

Link 

http://dx.doi.org/10.1016/j.bbalip.2014.08.008

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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