NonO Binds to the CpG Island of oct4 Promoter and Functions as a Transcriptional Activator of oct4 Gene Expression

Park, Yoojin; Lee, Ja Myong; Hwang, Min Young; Son, Gi Hoon; Geum, Dongho

doi:10.1007/s10059-013-2273-1

Cited by 24 publications

(24 citation statements)

References 48 publications

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“…DBHS proteins are nuclear proteins forming homo- and heterodimers in vivo 1,2 , and previous literature documents their involvement in various aspects of RNA metabolism 3 . Studies in vitro suggest that they act in transcriptional activation and repression 4-6 , splicing 7,8 , pre-mRNA processing 9 and RNA transport 10,11 . In addition, they are major components of nuclear paraspeckles, which have been recognized as nuclear RNA-holding structures for edited RNAs 12,13 that likely function in stress-mediated regulation via nuclear retention of transcripts 14-16 .…”

mentioning

confidence: 99%

Mutations in NONO lead to syndromic intellectual disability and inhibitory synaptic defects

Mircsof¹,

Langouët²,

Rio³

et al. 2015

Nat Neurosci

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The NONO protein has been characterized as an important transcriptional regulator in diverse cellular contexts. Here we show that loss of NONO function is a likely cause of human intellectual disability and that NONO-deficient mice have cognitive and affective deficits. Correspondingly, we find specific defects at inhibitory synapses, where NONO regulates synaptic transcription and gephyrin scaffold structure. Our data identify NONO as a possible neurodevelopmental disease gene and highlight the key role of the DBHS protein family in functional organization of GABAergic synapses.

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mentioning

confidence: 99%

Mutations in NONO lead to syndromic intellectual disability and inhibitory synaptic defects

Mircsof¹,

Langouët²,

Rio³

et al. 2015

Nat Neurosci

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“…As discussed, the para-speckle structure is absent in mESCs but Nono nonetheless is expressed and has been suggested to regulate transcription of Oct4 (Park et al, 2013), raising the possibility that Nono may play a role in regulating mESC pluripotency. To investigate this possibility, we first generated two independent Nono KO (KO1 and KO2) mESC lines using the CRISPR technology (Figure 1A and S1A).…”

Section: Resultsmentioning

confidence: 94%

“…Nono binds both DNA and RNA, possibly via its helix-turn-helix (HTH) and the RNA recognition motif (RRM) domains, and has been suggested to regulate transcription (Dong et al, 1993; Park et al, 2013; Yang et al, 1993). In differentiated cells, Nono, together with Pspc1, Psf and a scaffolding non-coding RNA, Neat1, forms the nuclear para-speckle structure, known to regulate RNA processing, nuclear retention of hyperedited mRNAs and stress responses induced by viral infection and DNA damage (Clemson et al, 2009; Fox et al, 2002; Fox and Lamond, 2010; Hutchinson et al, 2007; Li et al, 2009; Sunwoo et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Nono, a Bivalent Domain Factor, Regulates Erk Signaling and Mouse Embryonic Stem Cell Pluripotency

Karwacki-Neisius

Tang

et al. 2016

Cell Reports

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Summary Nono is a component of the para-speckle, which stores and processes RNA. Mouse embryonic stem cells (mESCs) lack para-speckles, leaving the function of Nono in mESCs unclear. Here we find that Nono functions as a chromatin regulator cooperating with Erk to regulate mESC pluripotency. We report that Nono loss results in robust self-renewing mESCs with epigenomic and transcriptomic features resembling the 2i (GSK and Erk inhibitors)-induced “ground state”. Erk interacts with and is required for Nono localization to a subset of bivalent genes that have high levels of poised RNA polymerase. Nono loss compromises Erk activation and RNA polymerase poising at its target bivalent genes in undifferentiated mESCs; thus disrupting target gene activation and differentiation. These findings argue that Nono collaborates with Erk signaling to regulate the integrity of bivalent domains and mESC pluripotency.

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“…In summary, the most likely explanation for the apparent inconsistencies between observations on DBHS protein assembly is that the extended coiled-coil/CSAH segment of DBHS proteins is highly versatile and can mediate a number of different interactions and multimerization modes in the different proteins in a context-dependent manner, as exemplified by the behavior of NONO/SFPQ tetramers and multimers depending on the ionic strength applied (Snijders et al 2015). Moreover, NONO can bind to specific DNA segments and is involved in transcriptional activation (Park et al 2013;Yadav et al 2014). NONO was shown to bind double-stranded DNA independently of RNA and single-stranded DNA (Yang et al 1993).…”

Section: Discussionmentioning

confidence: 99%

A conserved charged single α-helix with a putative steric role in paraspeckle formation

Dobson

Nyitray

Gáspári

2015

RNA

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Paraspeckles are subnuclear particles involved in the regulation of mRNA expression. They are formed by the association of DBHS family proteins and the NEAT1 long noncoding RNA. Here, we show that a recently identified structural motif, the charged single α-helix, is largely conserved in the DBHS family. Based on the available structural data and a previously suggested multimerization scheme of DBHS proteins, we built a structural model of a (PSPC1/NONO) n multimer that might have relevance in paraspeckle formation. Our model contains an extended coiled-coil region that is followed by and partially overlaps with the predicted charged single α-helix. We suggest that the charged single α-helix can act as an elastic ruler governing the exact positioning of the dimeric core structures relative to each other during paraspeckle assembly along the NEAT1 noncoding RNA.

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NonO Binds to the CpG Island of oct4 Promoter and Functions as a Transcriptional Activator of oct4 Gene Expression

Cited by 24 publications

References 48 publications

Mutations in NONO lead to syndromic intellectual disability and inhibitory synaptic defects

Mutations in NONO lead to syndromic intellectual disability and inhibitory synaptic defects

Nono, a Bivalent Domain Factor, Regulates Erk Signaling and Mouse Embryonic Stem Cell Pluripotency

A conserved charged single α-helix with a putative steric role in paraspeckle formation

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