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Review
. 2017 May;74(10):1805-1817.
doi: 10.1007/s00018-016-2438-0. Epub 2016 Dec 20.

Mechanisms of pluripotency maintenance in mouse embryonic stem cells

Chen-Yun Chen  1 , Yuan-Yuan Cheng  1   2 , Christopher Y T Yen  1 , Patrick C H Hsieh  3   4   5   6
Affiliations
Review

Mechanisms of pluripotency maintenance in mouse embryonic stem cells

Chen-Yun Chen et al. Cell Mol Life Sci. 2017 May.

Abstract

Mouse embryonic stem cells (mESCs), characterized by their pluripotency and capacity for self-renewal, are driven by a complex gene expression program composed of several regulatory mechanisms. These mechanisms collaborate to maintain the delicate balance of pluripotency gene expression and their disruption leads to loss of pluripotency. In this review, we provide an extensive overview of the key pillars of mESC pluripotency by elaborating on the various essential transcription factor networks and signaling pathways that directly or indirectly support this state. Furthermore, we consider the latest developments in the role of epigenetic regulation, such as noncoding RNA signaling or histone modifications.

Keywords: Epigenetic regulation; Mouse embryonic stem cells; Pluripotency; Transcriptional regulation.

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Figures

Fig. 1
Fig. 1
Regulation of key transcription factors for pluripotency maintenance of mouse embryonic stem cells
Fig. 2
Fig. 2
Regulation of major signaling pathways for pluripotency maintenance of mouse embryonic stem cells
Fig. 3
Fig. 3
Complexes-mediating histone modifications for pluripotency maintenance in mouse embryonic stem cells. Key subunits of PRC1 complexes are Cbx (Cbx2/4/6/7/8), Ring1A/B, Phc (Phc1/2/3), and Pcgf1/6. Ring1A/B are ubiquitin ligases responsible for ubiquitylization of lysine 119 of Histone 2A. Key subunits of PRC2 complexes are Ezh1/2, Suz12, Eed, and RbAp46/48. Ezh1/2 are methyltransferases responsible for di- or tri-methylation of lysine 27 of Histone 3. MLL is composed of Wdr5, Ash2l, and Rbbp5. MLL is a histone methyltransferase responsible for tri-methylation of lysine 4 of Histone 3
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