Phosphorylation of the Menin Tumor Suppressor Protein on Serine 543 and Serine 583

MacConaill, Laura E.; Hughes, Christina; Rozenblatt-Rosen, Orit; Nannepaga, Suraj; Meyerson, Matthew

doi:10.1158/1541-7786.mcr-06-0123

Cited by 20 publications

(20 citation statements)

References 39 publications

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“…Further, Kaikkonen et al demonstrated that transcription-coupled H3K4 methylation at de novo enhancers was mediated by members of the Mll family of histone methyltransferases. These fi ndings are consistent with the ability of Mlls to associate with the phosphorylated C terminal domain (CTD) of Pol II (Hughes et al 2004 ;Krogan et al 2003 ;MacConaill et al 2006 ;Milne et al 2005 ;Ng et al 2003 ;Rana et al 2011 ;Wood et al 2003 ) and suggest that the progressive accumulation of H3K4 methylation at de novo enhancers results from their association with active forms of Pol II (Fig. 12.4 ).…”

Section: An Order Of Events For Enhancer Transcriptionsupporting

confidence: 72%

Macrophage Activation as a Model System for Understanding Enhancer Transcription and eRNA Function

Allison

Glass

2015

Long Noncoding RNAs

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Macrophages are innate immune cells that sense the presence of pathogens through conserved pattern recognition receptors, which include TLR4. Activation of TLR4 by bacterial lipopolysaccharide induces the expression of thousands of genes that function to initiate infl ammation and coordinate innate and adaptive immune responses. Transcriptional activation of TLR4-responsive genes is mediated by signal-dependent transcription factors, such as NFκB, which bind to DNA regulatory elements termed enhancers. Recent fi ndings indicate that macrophage enhancers are actively transcribed in concert with nearby genes. Similar observations have been reported for other cell types, raising the general question of whether enhancer transcription and/or the resulting enhancer RNAs (eRNAs) are of functional importance. Here, we review the use of macrophage activation as an experimental system for addressing these questions and highlight areas for future research.

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Section: An Order Of Events For Enhancer Transcriptionsupporting

confidence: 72%

Macrophage Activation as a Model System for Understanding Enhancer Transcription and eRNA Function

Allison

Glass

2015

Long Noncoding RNAs

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“…2) Activating protein 2 delta (AP2δ) transcription factor, which is one of AP2 five family members (AP2α, AP2β, AP2γ, AP2δ and AP2ε), recruits Ash2I and ALR to the HOXC8 locus, resulting in H3K4me3-mediated gene activation (Tan et al, 2008). 3) Menin, which is a tumor suppressor gene associated with a syndrome known as multiple endocrine neoplasia type 1, binds to HOXC8 locus by associating with a histone methyltransferase complex containing two trithorax family proteins, MLL2 and Ash2L (MacConaill et al, 2006). 4) GTF2IRD1, which is a TFII-I family of transcription factors, interacts with HOXC8 early enhancer and represses the gene transcription (Thompson et al, 2007).…”

Section: Hoxc8 (Homeobox C8)mentioning

confidence: 99%

HOXC8 (homeobox C8)

Huang¹,

Li²

2015

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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“…The first phosphorylation modification of menin was found in 2006 by Matthew Meyerson group (MacConaill, et al 2006). Protein phosphorylation is considered to be the most abundant posttranslational modification in eukaryotes.…”

Section: Introductionmentioning

confidence: 99%

“…They initially found that menin migrated as a doublet on SDS-PAGE gels, indicating a possible posttranslational modification (Hughes et al 2004). Further study showed that menin is phosphorylated on two serine residues, Ser543 and Ser583 (MacConaill et al 2006). However, the functional study of the phosphorylation by mutating both serine residues had no impact on menin’s ability to recruit trithorax family complex proteins Ash2L, Rbbp5, and MLL2, nor on cell proliferation (MacConaill et al 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Further study showed that menin is phosphorylated on two serine residues, Ser543 and Ser583 (MacConaill et al 2006). However, the functional study of the phosphorylation by mutating both serine residues had no impact on menin’s ability to recruit trithorax family complex proteins Ash2L, Rbbp5, and MLL2, nor on cell proliferation (MacConaill et al 2006). While these two phosphorylation sites are situated between the two NLSs located at the C-terminal part of menin, mutations at both of the serine residues do not affect menin localization into the nucleus (MacConaill et al 2006).…”

Section: Introductionmentioning

confidence: 99%

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Epigenetic regulation by the menin pathway

Feng¹,

Ma²,

Hua³

2017

Endocrine-Related Cancer

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There is a trend of increasing prevalence of neuroendocrine tumors (NETs), and the inherited multiple endocrine neoplasia type 1 (MEN1) syndrome serves as a genetic model to investigate how NETs develop and the underlying mechanisms. Menin, encoded by the MEN1 gene, at least partly acts as a scaffold protein by interacting with multiple partners to regulate cellular homeostasis of various endocrine organs. Menin has multiple functions including regulating several important signaling pathways by controlling gene transcription. Here, we focus on reviewing the recent progress in elucidating the key biochemical role of menin in epigenetic regulation of gene transcription and cell signaling, as well as posttranslational regulation of menin itself. In particular, we will review the progress in studying structural and functional interactions of menin with various histone modifiers and transcription factors such as MLL, PRMT5, SUV39H1 and other transcription factors including c-Myb and JunD. Moreover, the role of menin in regulating cell signaling pathways such as TGF-beta, Wnt, and Hedgehog, as well as miRNA biogenesis and processing will be described. Further, the regulation of the MEN1 gene transcription, posttranslational modifications and stability of menin protein will be reviewed. These various modes of regulation by menin as well as regulation of menin by various biological factors broaden the view regarding how menin controls various biological processes in neuroendocrine organ homeostasis.

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Phosphorylation of the Menin Tumor Suppressor Protein on Serine 543 and Serine 583

Abstract: Multiple endocrine neoplasia type 1 (MEN-1)

Cited by 20 publications

References 39 publications

Macrophage Activation as a Model System for Understanding Enhancer Transcription and eRNA Function

Macrophage Activation as a Model System for Understanding Enhancer Transcription and eRNA Function

HOXC8 (homeobox C8)

Epigenetic regulation by the menin pathway

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