Identification of a putative transactivation domain in human Nanog

Oh, Jonghyun; Do, Hyun-Jin; Yang, Hyun Ok; Moon, Shin-Yong; Cha, Kwang-Yul; Chung, Hyung-Min; Kim, Jaehwan

doi:10.1038/emm.2005.33

Cited by 41 publications

(35 citation statements)

References 12 publications

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“…When fused to the DNA-binding domain of Gal4, both N-and C-terminal domains show trans-activator function [23], but the activity of the C-terminal domain is much higher (at least seven times) than the N-terminal domain [23]. Similar analysis on human Nanog protein reveals that only the C-terminal domain has transcriptional activity [24], suggesting that the C-terminal domain is functionally dominant. The prominent feature of the C-terminal domain is the presence of a 10 pentapeptide repeat (WR), each starting with a tryptophan (W).…”

Section: Nanog Is a Unique Homeobox Transcription Factormentioning

confidence: 89%

Nanog and transcriptional networks in embryonic stem cell pluripotency

2007

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Several extrinsic signals such as LIF, BMP and Wnt can support the self-renewal and pluripotency of embryonic stem (ES) cells through regulating the "pluripotent genes." A unique homeobox transcription factor, Nanog, is one of the key downstream effectors of these signals. Elevated level of Nanog can maintain the mouse ES cell self-renewal independent of LIF and enable human ES cell growth without feeder cells. In addition to the external signal pathways, intrinsic transcription factors such as FoxD3, P53 and Oct4 are also involved in regulating the expression of Nanog. Functionally, Nanog works together with other key pluripotent factors such as Oct4 and Sox2 to control a set of target genes that have important functions in ES cell pluripotency. These key factors form a regulatory network to support or limit each other's expression level, which maintains the properties of ES cells.

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Section: Nanog Is a Unique Homeobox Transcription Factormentioning

confidence: 89%

Nanog and transcriptional networks in embryonic stem cell pluripotency

2007

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“…Transactivation activity of NANOG can be mediated via the C-terminal WR and CD2 domains (Supplemental Fig. 6A; Pan and Pei 2003;Oh et al 2005). We hypothesized that the recruitment of the transactivation domains to major satellite repeats could underlie the open PCH organization typical of ESCs.…”

Section: The Nanog Transactivation Domain Is Critical For Heterochrommentioning

confidence: 99%

The pluripotency factor Nanog regulates pericentromeric heterochromatin organization in mouse embryonic stem cells

et al. 2016

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An open and decondensed chromatin organization is a defining property of pluripotency. Several epigenetic regulators have been implicated in maintaining an open chromatin organization, but how these processes are connected to the pluripotency network is unknown. Here, we identified a new role for the transcription factor NANOG as a key regulator connecting the pluripotency network with constitutive heterochromatin organization in mouse embryonic stem cells. Deletion of Nanog leads to chromatin compaction and the remodeling of heterochromatin domains. Forced expression of NANOG in epiblast stem cells is sufficient to decompact chromatin. NANOG associates with satellite repeats within heterochromatin domains, contributing to an architecture characterized by highly dispersed chromatin fibers, low levels of H3K9me3, and high major satellite transcription, and the strong transactivation domain of NANOG is required for this organization. The heterochromatin-associated protein SALL1 is a direct cofactor for NANOG, and loss of Sall1 recapitulates the Nanog-null phenotype, but the loss of Sall1 can be circumvented through direct recruitment of the NANOG transactivation domain to major satellites. These results establish a direct connection between the pluripotency network and chromatin organization and emphasize that maintaining an open heterochromatin architecture is a highly regulated process in embryonic stem cells.

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“…Murine and human Nanog were described as 3-domain proteins containing a homeodomain (HD), a serine enriched N-terminal, and a C-terminal transactivator domain containing several tryptophan repeats [40,41]. The tryptophan repeats were shown to be crucial for dimerization, proliferation, the maintenance of Nanog-dependent cell selfrenewal, and for binding of Nac1 [42][43][44].…”

Section: Divergence Of Nanog Proteins In Different Species and Relatimentioning

confidence: 99%