Menin - Revision history

Dmitry Dzhagarov at 10:41, 21 September 2024

2024-09-21T10:41:46Z

← Older revision		Revision as of 10:41, 21 September 2024
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	<ref>Ren, F., Guo, Q., & Zhou, H. (2023). Menin represses the proliferation of gastric cancer cells by interacting with IQGAP1. Biomedical Reports, 18(4), 1-7. </ref>		<ref>Ren, F., Guo, Q., & Zhou, H. (2023). Menin represses the proliferation of gastric cancer cells by interacting with IQGAP1. Biomedical Reports, 18(4), 1-7. </ref>

	MEN1 is an essential antifibrotic factor in renal fibrogenesis and could be a potential target for antifibrotic therapy. Since knockout of MEN1 resulted in chronic renal fibrosis and unilateral ureteral obstruction (UUO)-induced tubulointerstitial fibrosis (TIF), which is associated with an increased induction of epithelial-to-mesenchymal transition (EMT), G2/M arrest and JNK signaling. Mechanistically, menin recruits and increases H3K4me3 at the promoter regions of hepatocyte growth factor (HGF) and a disintegrin and metalloproteinase with thrombospondin motifs 5 (Adamts5) genes and enhances their transcriptional activation.<ref>Jin, B., Zhu, J., Zhou, Y., Liang, L., Yang, Y., Xu, L., ... & Li, H. (2022). Loss of MEN1 leads to renal fibrosis and decreases HGF‐Adamts5 pathway activity via an epigenetic mechanism. Clinical and Translational Medicine, 12(8), e982. PMID: 35968938 PMCID: PMC9377152 DOI: 10.1002/ctm2.982</ref>		MEN1 is an essential antifibrotic factor in renal fibrogenesis and could be a potential target for antifibrotic therapy. Since knockout of MEN1 resulted in chronic renal fibrosis and unilateral ureteral obstruction (UUO)-induced tubulointerstitial fibrosis (TIF), which is associated with an increased induction of epithelial-to-mesenchymal transition (EMT), G2/M arrest and [[Role of JNK in aging\|JNK]] signaling. Mechanistically, menin recruits and increases H3K4me3 at the promoter regions of hepatocyte growth factor (HGF) and a disintegrin and metalloproteinase with thrombospondin motifs 5 (Adamts5) genes and enhances their transcriptional activation.<ref>Jin, B., Zhu, J., Zhou, Y., Liang, L., Yang, Y., Xu, L., ... & Li, H. (2022). Loss of MEN1 leads to renal fibrosis and decreases HGF‐Adamts5 pathway activity via an epigenetic mechanism. Clinical and Translational Medicine, 12(8), e982. PMID: 35968938 PMCID: PMC9377152 DOI: 10.1002/ctm2.982</ref>
	The levels of menin by degrees diminish with the progression of fibrosis in a mouse model of radiation‐induced pulmonary fibrosis. MEN1 plays a key role in the formation of pulmonary fibrosis by regulating the secretion of TGF-β and the activation of TGF-β/Smads signaling pathway.<ref>Wei, W., Zhang, H. Y., Gong, X. K., Dong, Z., Chen, Z. Y., Wang, R., ... & Jin, S. Z. (2018). Mechanism of MEN1 gene in radiation-induced pulmonary fibrosis in mice. Gene, 678, 252-260. PMID: 30099020 DOI: 10.1016/j.gene.2018.08.039</ref>		The levels of menin by degrees diminish with the progression of fibrosis in a mouse model of radiation‐induced pulmonary fibrosis. MEN1 plays a key role in the formation of pulmonary fibrosis by regulating the secretion of TGF-β and the activation of TGF-β/Smads signaling pathway.<ref>Wei, W., Zhang, H. Y., Gong, X. K., Dong, Z., Chen, Z. Y., Wang, R., ... & Jin, S. Z. (2018). Mechanism of MEN1 gene in radiation-induced pulmonary fibrosis in mice. Gene, 678, 252-260. PMID: 30099020 DOI: 10.1016/j.gene.2018.08.039</ref>

Andrea: Added category

2023-06-05T08:29:55Z

Added category

← Older revision		Revision as of 08:29, 5 June 2023
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	[[Category:Drafts]]		[[Category:Drafts]]
	[[Category:Longevity genes]]		[[Category:Longevity genes]]
			[[Category:Main list]]

Dmitry Dzhagarov at 16:58, 31 May 2023

2023-05-31T16:58:59Z

← Older revision		Revision as of 16:58, 31 May 2023
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	Menin represses MEN1 through inhibiting cell proliferation through multiple mechanisms.<ref>Wu, T., & Hua, X. (2011). Menin represses tumorigenesis via repressing cell proliferation. American journal of cancer research, 1(6), 726. PMID: 22016823 PMCID: PMC3195934</ref>		Menin represses MEN1 through inhibiting cell proliferation through multiple mechanisms.<ref>Wu, T., & Hua, X. (2011). Menin represses tumorigenesis via repressing cell proliferation. American journal of cancer research, 1(6), 726. PMID: 22016823 PMCID: PMC3195934</ref>
	1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.		1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.

			<ref>Ren, F., Guo, Q., & Zhou, H. (2023). Menin represses the proliferation of gastric cancer cells by interacting with IQGAP1. Biomedical Reports, 18(4), 1-7. </ref>

	MEN1 is an essential antifibrotic factor in renal fibrogenesis and could be a potential target for antifibrotic therapy. Since knockout of MEN1 resulted in chronic renal fibrosis and unilateral ureteral obstruction (UUO)-induced tubulointerstitial fibrosis (TIF), which is associated with an increased induction of epithelial-to-mesenchymal transition (EMT), G2/M arrest and JNK signaling. Mechanistically, menin recruits and increases H3K4me3 at the promoter regions of hepatocyte growth factor (HGF) and a disintegrin and metalloproteinase with thrombospondin motifs 5 (Adamts5) genes and enhances their transcriptional activation.<ref>Jin, B., Zhu, J., Zhou, Y., Liang, L., Yang, Y., Xu, L., ... & Li, H. (2022). Loss of MEN1 leads to renal fibrosis and decreases HGF‐Adamts5 pathway activity via an epigenetic mechanism. Clinical and Translational Medicine, 12(8), e982. PMID: 35968938 PMCID: PMC9377152 DOI: 10.1002/ctm2.982</ref>		MEN1 is an essential antifibrotic factor in renal fibrogenesis and could be a potential target for antifibrotic therapy. Since knockout of MEN1 resulted in chronic renal fibrosis and unilateral ureteral obstruction (UUO)-induced tubulointerstitial fibrosis (TIF), which is associated with an increased induction of epithelial-to-mesenchymal transition (EMT), G2/M arrest and JNK signaling. Mechanistically, menin recruits and increases H3K4me3 at the promoter regions of hepatocyte growth factor (HGF) and a disintegrin and metalloproteinase with thrombospondin motifs 5 (Adamts5) genes and enhances their transcriptional activation.<ref>Jin, B., Zhu, J., Zhou, Y., Liang, L., Yang, Y., Xu, L., ... & Li, H. (2022). Loss of MEN1 leads to renal fibrosis and decreases HGF‐Adamts5 pathway activity via an epigenetic mechanism. Clinical and Translational Medicine, 12(8), e982. PMID: 35968938 PMCID: PMC9377152 DOI: 10.1002/ctm2.982</ref>

Dmitry Dzhagarov at 15:57, 31 May 2023

2023-05-31T15:57:51Z

← Older revision		Revision as of 15:57, 31 May 2023
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	The expression of menin is reduced in the liver of aging mice. Hepatocyte-specific deletion of Men1 induces liver steatosis in aging mice. Menin deficiency promotes high-fat diet-induced liver steatosis in mice. Menin recruits SIRT1 to control hepatic CD36 expression and triglyceride accumulation through histone.<ref>Cao, Y., Xue, Y., Xue, L., Jiang, X., Wang, X., Zhang, Z., ... & Ning, G. (2013). Hepatic menin recruits SIRT1 to control liver steatosis through histone deacetylation. Journal of Hepatology, 59(6), 1299-1306. PMID: 23867312 DOI: 10.1016/j.jhep.2013.07.011</ref>		The expression of menin is reduced in the liver of aging mice. Hepatocyte-specific deletion of Men1 induces liver steatosis in aging mice. Menin deficiency promotes high-fat diet-induced liver steatosis in mice. Menin recruits SIRT1 to control hepatic CD36 expression and triglyceride accumulation through histone.<ref>Cao, Y., Xue, Y., Xue, L., Jiang, X., Wang, X., Zhang, Z., ... & Ning, G. (2013). Hepatic menin recruits SIRT1 to control liver steatosis through histone deacetylation. Journal of Hepatology, 59(6), 1299-1306. PMID: 23867312 DOI: 10.1016/j.jhep.2013.07.011</ref>

			Menin plays important roles in neuroinflammation and brain development.

	<ref>Matkar, S., Thiel, A., & Hua, X. (2013). Menin: a scaffold protein that controls gene expression and cell signaling. Trends in biochemical sciences, 38(8), 394-402. PMID: 23850066 PMCID: PMC3741089 DOI: 10.1016/j.tibs.2013.05.005</ref>		<ref>Matkar, S., Thiel, A., & Hua, X. (2013). Menin: a scaffold protein that controls gene expression and cell signaling. Trends in biochemical sciences, 38(8), 394-402. PMID: 23850066 PMCID: PMC3741089 DOI: 10.1016/j.tibs.2013.05.005</ref>
	<ref>Feng, Z., Ma, J., & Hua, X. (2017). Epigenetic regulation by the menin pathway. Endocrine-related cancer, 24(10), T147. PMID: 28811300 PMCID: PMC5612327 DOI: 10.1530/ERC-17-0298</ref>		<ref>Feng, Z., Ma, J., & Hua, X. (2017). Epigenetic regulation by the menin pathway. Endocrine-related cancer, 24(10), T147. PMID: 28811300 PMCID: PMC5612327 DOI: 10.1530/ERC-17-0298</ref>
	<ref>Leng, L., Yuan, Z., Su, X., Chen, Z., Yang, S., Chen, M., ... & Zhang, J. (2023). Hypothalamic Menin regulates systemic aging and cognitive decline. Plos Biology, 21(3), e3002033. PMID: 36928253 PMCID: PMC10019680 DOI: 10.1371/journal.pbio.3002033</ref>
			'''The hypothalamic Menin signaling diminished in aged mice, which correlates with systemic aging''' and cognitive deficits.<ref name="Hypothal">Leng, L., Yuan, Z., Su, X., Chen, Z., Yang, S., Chen, M., ... & Zhang, J. (2023). Hypothalamic Menin regulates systemic aging and cognitive decline. Plos Biology, 21(3), e3002033. PMID: 36928253 PMCID: PMC10019680 DOI: 10.1371/journal.pbio.3002033</ref> '''Restoring Menin expression in ventromedial nucleus of hypothalamus (VMH) of aged mice extended lifespan, improved learning and memory, and ameliorated aging biomarkers''', while inhibiting Menin in VMH of middle-aged mice induced premature aging and accelerated cognitive decline. Menin epigenetically regulates neuroinflammatory and metabolic pathways, including D-serine metabolism.<ref name="Hypothal" /> Aging-associated Menin reduction led to impaired D-serine release by VMH-hippocampus neural circuit, while D-serine supplement rescued cognitive decline in aged mice. Collectively, VMH Menin serves as a key regulator of systemic aging and aging-related cognitive decline.<ref name="Hypothal" />


	Methylation of histone H3 lysine-79 (H3K79) plays key roles in gene regulation. The protein menin was identified as a reader of H3K79me2.<ref>Yang, Y. J., Song, T. Y., Park, J., Lee, J., Lim, J., Jang, H., ... & Cho, E. J. (2013). Menin mediates epigenetic regulation via histone H3 lysine 9 methylation. Cell death & disease, 4(4), e583-e583. PMID: 23579270 PMCID: PMC3668625 DOI: 10.1038/cddis.2013.98</ref><ref>Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W. H., ... & Li, X. D. (2023). Menin “reads” H3K79me2 mark in a nucleosomal context. Science, 379(6633), 717-723. PMID: 36795828 DOI: 10.1126/science.adc9318</ref>		Methylation of histone H3 lysine-79 (H3K79) plays key roles in gene regulation. The protein menin was identified as a reader of H3K79me2.<ref>Yang, Y. J., Song, T. Y., Park, J., Lee, J., Lim, J., Jang, H., ... & Cho, E. J. (2013). Menin mediates epigenetic regulation via histone H3 lysine 9 methylation. Cell death & disease, 4(4), e583-e583. PMID: 23579270 PMCID: PMC3668625 DOI: 10.1038/cddis.2013.98</ref><ref>Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W. H., ... & Li, X. D. (2023). Menin “reads” H3K79me2 mark in a nucleosomal context. Science, 379(6633), 717-723. PMID: 36795828 DOI: 10.1126/science.adc9318</ref>

Dmitry Dzhagarov at 15:39, 31 May 2023

2023-05-31T15:39:11Z

← Older revision		Revision as of 15:39, 31 May 2023
Line 15:		Line 15:
	1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.		1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.

			MEN1 is an essential antifibrotic factor in renal fibrogenesis and could be a potential target for antifibrotic therapy. Since knockout of MEN1 resulted in chronic renal fibrosis and unilateral ureteral obstruction (UUO)-induced tubulointerstitial fibrosis (TIF), which is associated with an increased induction of epithelial-to-mesenchymal transition (EMT), G2/M arrest and JNK signaling. Mechanistically, menin recruits and increases H3K4me3 at the promoter regions of hepatocyte growth factor (HGF) and a disintegrin and metalloproteinase with thrombospondin motifs 5 (Adamts5) genes and enhances their transcriptional activation.<ref>Jin, B., Zhu, J., Zhou, Y., Liang, L., Yang, Y., Xu, L., ... & Li, H. (2022). Loss of MEN1 leads to renal fibrosis and decreases HGF‐Adamts5 pathway activity via an epigenetic mechanism. Clinical and Translational Medicine, 12(8), e982. PMID: 35968938 PMCID: PMC9377152 DOI: 10.1002/ctm2.982</ref>
			The levels of menin by degrees diminish with the progression of fibrosis in a mouse model of radiation‐induced pulmonary fibrosis. MEN1 plays a key role in the formation of pulmonary fibrosis by regulating the secretion of TGF-β and the activation of TGF-β/Smads signaling pathway.<ref>Wei, W., Zhang, H. Y., Gong, X. K., Dong, Z., Chen, Z. Y., Wang, R., ... & Jin, S. Z. (2018). Mechanism of MEN1 gene in radiation-induced pulmonary fibrosis in mice. Gene, 678, 252-260. PMID: 30099020 DOI: 10.1016/j.gene.2018.08.039</ref>

			The expression of menin is reduced in the liver of aging mice. Hepatocyte-specific deletion of Men1 induces liver steatosis in aging mice. Menin deficiency promotes high-fat diet-induced liver steatosis in mice. Menin recruits SIRT1 to control hepatic CD36 expression and triglyceride accumulation through histone.<ref>Cao, Y., Xue, Y., Xue, L., Jiang, X., Wang, X., Zhang, Z., ... & Ning, G. (2013). Hepatic menin recruits SIRT1 to control liver steatosis through histone deacetylation. Journal of Hepatology, 59(6), 1299-1306. PMID: 23867312 DOI: 10.1016/j.jhep.2013.07.011</ref>

	<ref>Matkar, S., Thiel, A., & Hua, X. (2013). Menin: a scaffold protein that controls gene expression and cell signaling. Trends in biochemical sciences, 38(8), 394-402. PMID: 23850066 PMCID: PMC3741089 DOI: 10.1016/j.tibs.2013.05.005</ref>		<ref>Matkar, S., Thiel, A., & Hua, X. (2013). Menin: a scaffold protein that controls gene expression and cell signaling. Trends in biochemical sciences, 38(8), 394-402. PMID: 23850066 PMCID: PMC3741089 DOI: 10.1016/j.tibs.2013.05.005</ref>

Dmitry Dzhagarov at 11:31, 31 May 2023

2023-05-31T11:31:53Z

← Older revision		Revision as of 11:31, 31 May 2023
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	! MEN1		! MEN1
	\|-		\|-
	\| [https://www.ncbi.nlm.nih.gov/gene MEN1 menin 1 [ Homo sapiens (human) ]		\| [https://www.ncbi.nlm.nih.gov/gene MEN1 menin 1. Homo sapiens (human) Gene ID: 4221]
	Gene ID: 4221]
	\|-		\|-
	\| [https://www.ncbi.nlm.nih.gov/nuccore/U93236.1 Human menin (MEN1) mRNA], complete cds		\| [https://www.ncbi.nlm.nih.gov/nuccore/U93236.1 Human menin (MEN1) mRNA], complete cds GenBank: U93236.1
	GenBank: U93236.1
	\|-		\|-
	~~\| [[File:3u84menin.png~~\|Crystal Structure of Human Menin. ~~under license CC BY-SA 3~~.0]]		\| Crystal Structure of Human Menin. [https://www.rcsb.org/structure/3U84 3U84]
	\|}		\|}
	'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Guru, S. C., Goldsmith, P. K., Burns, A. L., Marx, S. J., Spiegel, A. M., Collins, F. S., & Chandrasekharappa, S. C. (1998). Menin, the product of the MEN1 gene, is a nuclear protein. Proceedings of the National Academy of Sciences, 95(4), 1630-1634. PMID: 9465067 PMCID: PMC19125 DOI: 10.1073/pnas.95.4.1630</ref><ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref> Multiple endocrine neoplasia type 1 (MEN1) is an autosomal dominantly inherited endocrine disease (famous as Wermer disease) in which more than one endocrine gland develops tumors or grows excessively without forming tumors as a consequence of the MEN1 gene mutation.<ref>Bale, A. E., Norton, J. A., Wong, E. L., Fryburg, J. S., Maton, P. N., Oldfield, E. H., ... & Marx, S. J. (1991). Allelic Loss on Chromosome 11 in Hereditary and Sporadic Tumors Related to Familial Multiple Endocrine Neoplasia Type. Cancer research, 51(4), 1154-1157. PMID: 1671755</ref>		'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Guru, S. C., Goldsmith, P. K., Burns, A. L., Marx, S. J., Spiegel, A. M., Collins, F. S., & Chandrasekharappa, S. C. (1998). Menin, the product of the MEN1 gene, is a nuclear protein. Proceedings of the National Academy of Sciences, 95(4), 1630-1634. PMID: 9465067 PMCID: PMC19125 DOI: 10.1073/pnas.95.4.1630</ref><ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref> Multiple endocrine neoplasia type 1 (MEN1) is an autosomal dominantly inherited endocrine disease (famous as Wermer disease) in which more than one endocrine gland develops tumors or grows excessively without forming tumors as a consequence of the MEN1 gene mutation.<ref>Bale, A. E., Norton, J. A., Wong, E. L., Fryburg, J. S., Maton, P. N., Oldfield, E. H., ... & Marx, S. J. (1991). Allelic Loss on Chromosome 11 in Hereditary and Sporadic Tumors Related to Familial Multiple Endocrine Neoplasia Type. Cancer research, 51(4), 1154-1157. PMID: 1671755</ref>

Dmitry Dzhagarov at 10:40, 31 May 2023

2023-05-31T10:40:38Z

@@ Line 1: / Line 1: @@
 '''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Guru, S. C., Goldsmith, P. K., Burns, A. L., Marx, S. J., Spiegel, A. M., Collins, F. S., & Chandrasekharappa, S. C. (1998). Menin, the product of the MEN1 gene, is a nuclear protein. Proceedings of the National Academy of Sciences, 95(4), 1630-1634. PMID: 9465067 PMCID: PMC19125 DOI: 10.1073/pnas.95.4.1630</ref><ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref>  Multiple endocrine neoplasia type 1 (MEN1) is an autosomal dominantly inherited endocrine disease (famous as Wermer disease) in which more than one endocrine gland develops tumors or grows excessively without forming tumors as a consequence of the MEN1 gene mutation.<ref>Bale, A. E., Norton, J. A., Wong, E. L., Fryburg, J. S., Maton, P. N., Oldfield, E. H., ... & Marx, S. J. (1991). Allelic Loss on Chromosome 11 in Hereditary and Sporadic Tumors Related to Familial Multiple Endocrine Neoplasia Type. Cancer research, 51(4), 1154-1157. PMID: 1671755</ref>
 Menin represses MEN1 through inhibiting cell proliferation through multiple mechanisms.<ref>Wu, T., & Hua, X. (2011). Menin represses tumorigenesis via repressing cell proliferation. American journal of cancer research, 1(6), 726.  PMID: 22016823 PMCID: PMC3195934</ref>
@@ Line 10: / Line 24: @@
 Methylation of histone H3 lysine-79 (H3K79) plays key roles in gene regulation. The protein menin was identified as a reader of H3K79me2.<ref>Yang, Y. J., Song, T. Y., Park, J., Lee, J., Lim, J., Jang, H., ... & Cho, E. J. (2013). Menin mediates epigenetic regulation via histone H3 lysine 9 methylation. Cell death & disease, 4(4), e583-e583. PMID: 23579270 PMCID: PMC3668625 DOI: 10.1038/cddis.2013.98</ref><ref>Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W. H., ... & Li, X. D. (2023). Menin “reads” H3K79me2 mark in a nucleosomal context. Science, 379(6633), 717-723.  PMID: 36795828 DOI: 10.1126/science.adc9318</ref>
+<ref>Agarwal, S. K. (2017). The future: genetics advances in MEN1 therapeutic approaches and management strategies. Endocrine-related cancer, 24(10), T119. PMID: 28899949 PMCID: PMC5679100 DOI: 10.1530/ERC-17-0199</ref>
 == References ==

Dmitry Dzhagarov at 06:10, 31 May 2023

2023-05-31T06:10:38Z

← Older revision		Revision as of 06:10, 31 May 2023
Line 1:		Line 1:
	'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref> Multiple endocrine neoplasia type 1 (MEN1) is an autosomal dominantly inherited endocrine disease (famous as Wermer disease) in which more than one endocrine gland develops tumors or grows excessively without forming tumors as a consequence of the MEN1 gene mutation.<ref>Bale, A. E., Norton, J. A., Wong, E. L., Fryburg, J. S., Maton, P. N., Oldfield, E. H., ... & Marx, S. J. (1991). Allelic Loss on Chromosome 11 in Hereditary and Sporadic Tumors Related to Familial Multiple Endocrine Neoplasia Type. Cancer research, 51(4), 1154-1157. PMID: 1671755</ref>		'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Guru, S. C., Goldsmith, P. K., Burns, A. L., Marx, S. J., Spiegel, A. M., Collins, F. S., & Chandrasekharappa, S. C. (1998). Menin, the product of the MEN1 gene, is a nuclear protein. Proceedings of the National Academy of Sciences, 95(4), 1630-1634. PMID: 9465067 PMCID: PMC19125 DOI: 10.1073/pnas.95.4.1630</ref><ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref> Multiple endocrine neoplasia type 1 (MEN1) is an autosomal dominantly inherited endocrine disease (famous as Wermer disease) in which more than one endocrine gland develops tumors or grows excessively without forming tumors as a consequence of the MEN1 gene mutation.<ref>Bale, A. E., Norton, J. A., Wong, E. L., Fryburg, J. S., Maton, P. N., Oldfield, E. H., ... & Marx, S. J. (1991). Allelic Loss on Chromosome 11 in Hereditary and Sporadic Tumors Related to Familial Multiple Endocrine Neoplasia Type. Cancer research, 51(4), 1154-1157. PMID: 1671755</ref>
	Menin represses MEN1 through inhibiting cell proliferation through multiple mechanisms.<ref>Wu, T., & Hua, X. (2011). Menin represses tumorigenesis via repressing cell proliferation. American journal of cancer research, 1(6), 726. PMID: 22016823 PMCID: PMC3195934</ref>		Menin represses MEN1 through inhibiting cell proliferation through multiple mechanisms.<ref>Wu, T., & Hua, X. (2011). Menin represses tumorigenesis via repressing cell proliferation. American journal of cancer research, 1(6), 726. PMID: 22016823 PMCID: PMC3195934</ref>
	1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.		1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.


			<ref>Matkar, S., Thiel, A., & Hua, X. (2013). Menin: a scaffold protein that controls gene expression and cell signaling. Trends in biochemical sciences, 38(8), 394-402. PMID: 23850066 PMCID: PMC3741089 DOI: 10.1016/j.tibs.2013.05.005</ref>
			<ref>Feng, Z., Ma, J., & Hua, X. (2017). Epigenetic regulation by the menin pathway. Endocrine-related cancer, 24(10), T147. PMID: 28811300 PMCID: PMC5612327 DOI: 10.1530/ERC-17-0298</ref>
			<ref>Leng, L., Yuan, Z., Su, X., Chen, Z., Yang, S., Chen, M., ... & Zhang, J. (2023). Hypothalamic Menin regulates systemic aging and cognitive decline. Plos Biology, 21(3), e3002033. PMID: 36928253 PMCID: PMC10019680 DOI: 10.1371/journal.pbio.3002033</ref>

			Methylation of histone H3 lysine-79 (H3K79) plays key roles in gene regulation. The protein menin was identified as a reader of H3K79me2.<ref>Yang, Y. J., Song, T. Y., Park, J., Lee, J., Lim, J., Jang, H., ... & Cho, E. J. (2013). Menin mediates epigenetic regulation via histone H3 lysine 9 methylation. Cell death & disease, 4(4), e583-e583. PMID: 23579270 PMCID: PMC3668625 DOI: 10.1038/cddis.2013.98</ref><ref>Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W. H., ... & Li, X. D. (2023). Menin “reads” H3K79me2 mark in a nucleosomal context. Science, 379(6633), 717-723. PMID: 36795828 DOI: 10.1126/science.adc9318</ref>

Dmitry Dzhagarov: Created page with "'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0 Multiple endocrine neoplasia type 1 (MEN1) is an..."

2023-05-31T04:18:03Z

Created page with "'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref> Multiple endocrine neoplasia type 1 (MEN1) is an..."

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'''Menin''' is a 610-amino acid nuclear protein that in humans is encoded by the '''MEN1 (multiple endocrine neoplasia type 1) gene''', located on long arm of chromosome 11 (11q13).<ref>Larsson, C., Skogseid, B., Öberg, K., Nakamura, Y., & Nordenskjöld, M. (1988). Multiple endocrine neoplasia type 1 gene maps to chromosome 11 and is lost in insulinoma. Nature, 332(6159), 85-87. PMID: 2894610 DOI: 10.1038/332085a0</ref> Multiple endocrine neoplasia type 1 (MEN1) is an autosomal dominantly inherited endocrine disease (famous as Wermer disease) in which more than one endocrine gland develops tumors or grows excessively without forming tumors as a consequence of the MEN1 gene mutation.<ref>Bale, A. E., Norton, J. A., Wong, E. L., Fryburg, J. S., Maton, P. N., Oldfield, E. H., ... & Marx, S. J. (1991). Allelic Loss on Chromosome 11 in Hereditary and Sporadic Tumors Related to Familial Multiple Endocrine Neoplasia Type. Cancer research, 51(4), 1154-1157. PMID: 1671755</ref>
Menin represses MEN1 through inhibiting cell proliferation through multiple mechanisms.<ref>Wu, T., & Hua, X. (2011). Menin represses tumorigenesis via repressing cell proliferation. American journal of cancer research, 1(6), 726. PMID: 22016823 PMCID: PMC3195934</ref>
1) Menin interacts with various histonemodifying enzymes, such as MLL, EZH2 and HDACs, to affect gene transcription, leading to repression of cell proliferation. 2) Menin also interacts with various transcription factors, such as JunD, NF-κB, PPARγ and VDR, to induce or suppress gene transcription. As these various transcription factors are known to regulate cell proliferation, their interaction with menin may be relevant to menin's role in inhibiting cell proliferation. 3) Menin inhibits cell proliferation via TGF-β signaling and Wnt/β-catenin signaling pathways. 4) Menin represses certain pro-proliferative factors involved in endocrine tumors such as IGFBP-2, IGF2 and PTHrP to repress cell proliferation. 5) Menin affects cell cycle progression to inhibit cell proliferation.

== References ==
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[[Category:Drafts]]
[[Category:Longevity genes]]