Home > Publications Database > Histone-methyltransferase MLL2 (KMT2B) is required for memory formation in mice. > print

001     136804
005     20240321220134.0
024 7 _ |a 10.1523/JNEUROSCI.3356-12.2013
|2 doi
024 7 _ |a pmid:23426673
|2 pmid
024 7 _ |a pmc:PMC6619533
|2 pmc
024 7 _ |a 0270-6474
|2 ISSN
024 7 _ |a 1529-2401
|2 ISSN
024 7 _ |a altmetric:1710562
|2 altmetric
037 _ _ |a DZNE-2020-03126
041 _ _ |a English
082 _ _ |a 610
100 1 _ |a Kerimoglu, Cemil
|0 P:(DE-2719)2812366
|b 0
|e First author
|u dzne
245 _ _ |a Histone-methyltransferase MLL2 (KMT2B) is required for memory formation in mice.
260 _ _ |a Washington, DC
|c 2013
|b Soc.57413
264 _ 1 |3 online
|2 Crossref
|b Society for Neuroscience
|c 2013-02-20
264 _ 1 |3 print
|2 Crossref
|b Society for Neuroscience
|c 2013-02-20
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|b journal
|m journal
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|s 1690466513_8967
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a The consolidation of long-term memories requires differential gene expression. Recent research has suggested that dynamic changes in chromatin structure play a role in regulating the gene expression program linked to memory formation. The contribution of histone methylation, an important regulatory mechanism of chromatin plasticity that is mediated by the counteracting activity of histone-methyltransferases and histone-demethylases, is, however, not well understood. Here we show that mice lacking the histone-methyltransferase myeloid/lymphoid or mixed-lineage leukemia 2 (mll2/kmt2b) gene in adult forebrain excitatory neurons display impaired hippocampus-dependent memory function. Consistent with the role of KMT2B in gene-activation DNA microarray analysis revealed that 152 genes were downregulated in the hippocampal dentate gyrus region of mice lacking kmt2b. Downregulated plasticity genes showed a specific deficit in histone 3 lysine 4 di- and trimethylation, while histone 3 lysine 4 monomethylation was not affected. Our data demonstrates that KMT2B mediates hippocampal histone 3 lysine 4 di- and trimethylation and is a critical player for memory formation.
536 _ _ |a 342 - Disease Mechanisms and Model Systems (POF3-342)
|0 G:(DE-HGF)POF3-342
|c POF3-342
|f POF III
|x 0
542 _ _ |i 2013-08-20
|2 Crossref
|u https://creativecommons.org/licenses/by-nc-sa/4.0/
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a DNA-Binding Proteins
|2 NLM Chemicals
650 _ 7 |a KMT2D protein, human
|2 NLM Chemicals
650 _ 7 |a Neoplasm Proteins
|2 NLM Chemicals
650 _ 7 |a Histone Methyltransferases
|0 EC 2.1.1.-
|2 NLM Chemicals
650 _ 7 |a Histone-Lysine N-Methyltransferase
|0 EC 2.1.1.43
|2 NLM Chemicals
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a DNA-Binding Proteins: deficiency
|2 MeSH
650 _ 2 |a DNA-Binding Proteins: genetics
|2 MeSH
650 _ 2 |a DNA-Binding Proteins: physiology
|2 MeSH
650 _ 2 |a Hippocampus: enzymology
|2 MeSH
650 _ 2 |a Histone Methyltransferases
|2 MeSH
650 _ 2 |a Histone-Lysine N-Methyltransferase: deficiency
|2 MeSH
650 _ 2 |a Histone-Lysine N-Methyltransferase: genetics
|2 MeSH
650 _ 2 |a Maze Learning: physiology
|2 MeSH
650 _ 2 |a Memory, Long-Term: physiology
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Mice, Inbred C57BL
|2 MeSH
650 _ 2 |a Mice, Knockout
|2 MeSH
650 _ 2 |a Mice, Transgenic
|2 MeSH
650 _ 2 |a Neoplasm Proteins: deficiency
|2 MeSH
650 _ 2 |a Neoplasm Proteins: genetics
|2 MeSH
650 _ 2 |a Neoplasm Proteins: physiology
|2 MeSH
650 _ 2 |a Neuronal Plasticity: genetics
|2 MeSH
650 _ 2 |a Neuronal Plasticity: physiology
|2 MeSH
700 1 _ |a Agis-Balboa, Roberto C
|0 P:(DE-2719)9000006
|b 1
|u dzne
700 1 _ |a Kranz, Andrea
|0 P:(DE-HGF)0
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700 1 _ |a Stilling, Roman
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700 1 _ |a Bahari-Javan, Sanaz
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700 1 _ |a Benito Garagorri, Eva
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700 1 _ |a Halder, Rashi
|0 P:(DE-2719)2810512
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700 1 _ |a Burkhardt, Susanne
|0 P:(DE-2719)2810773
|b 7
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700 1 _ |a Stewart, Adrian Francis
|0 P:(DE-HGF)0
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700 1 _ |a Fischer, Andre
|0 P:(DE-2719)2000047
|b 9
|e Last author
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773 1 8 |a 10.1523/jneurosci.3356-12.2013
|b Society for Neuroscience
|d 2013-02-20
|n 8
|p 3452-3464
|3 journal-article
|2 Crossref
|t The Journal of Neuroscience
|v 33
|y 2013
|x 0270-6474
773 _ _ |a 10.1523/JNEUROSCI.3356-12.2013
|g Vol. 33, no. 8, p. 3452 - 3464
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856 7 _ |2 Pubmed Central
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913 1 _ |a DE-HGF
|b Gesundheit
|l Erkrankungen des Nervensystems
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914 1 _ |y 2013
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