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@ARTICLE{Kerimoglu:136804,
author = {Kerimoglu, Cemil and Agis-Balboa, Roberto C and Kranz,
Andrea and Stilling, Roman and Bahari-Javan, Sanaz and
Benito Garagorri, Eva and Halder, Rashi and Burkhardt,
Susanne and Stewart, Adrian Francis and Fischer, Andre},
title = {{H}istone-methyltransferase {MLL}2 ({KMT}2{B}) is required
for memory formation in mice.},
journal = {The journal of neuroscience},
volume = {33},
number = {8},
issn = {0270-6474},
address = {Washington, DC},
publisher = {Soc.57413},
reportid = {DZNE-2020-03126},
pages = {3452-3464},
year = {2013},
abstract = {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.},
keywords = {Animals / DNA-Binding Proteins: deficiency / DNA-Binding
Proteins: genetics / DNA-Binding Proteins: physiology /
Hippocampus: enzymology / Histone Methyltransferases /
Histone-Lysine N-Methyltransferase: deficiency /
Histone-Lysine N-Methyltransferase: genetics / Maze
Learning: physiology / Memory, Long-Term: physiology / Mice
/ Mice, Inbred C57BL / Mice, Knockout / Mice, Transgenic /
Neoplasm Proteins: deficiency / Neoplasm Proteins: genetics
/ Neoplasm Proteins: physiology / Neuronal Plasticity:
genetics / Neuronal Plasticity: physiology / DNA-Binding
Proteins (NLM Chemicals) / KMT2D protein, human (NLM
Chemicals) / Neoplasm Proteins (NLM Chemicals) / Histone
Methyltransferases (NLM Chemicals) / Histone-Lysine
N-Methyltransferase (NLM Chemicals)},
cin = {AG Fischer ; AG Fischer / RNAome database ; AG Sananbenesi
; AG Sananbenesi / Göttingen common},
ddc = {610},
cid = {I:(DE-2719)1410002 / I:(DE-2719)1410004 /
I:(DE-2719)6000014},
pnm = {342 - Disease Mechanisms and Model Systems (POF3-342)},
pid = {G:(DE-HGF)POF3-342},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:23426673},
pmc = {pmc:PMC6619533},
doi = {10.1523/JNEUROSCI.3356-12.2013},
url = {https://pub.dzne.de/record/136804},
}