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| Kofi... |
 Posted: Tue Oct 27, 2009 10:41 pm |
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Proc Natl Acad Sci U S A. 2009 Jun 9;106(23):9447-52. Epub 2009 May 26.
Modulation of long-term memory for object recognition via HDAC
inhibition.
Stefanko DP, Barrett RM, Ly AR, Reolon GK, Wood MA.
Department of Neurobiology and Behavior, Center for the Neurobiology of
Learning and Memory, University of California, Irvine, CA 92697-3800,
USA.
Histone acetylation is a chromatin modification critically involved in
gene regulation during many neural processes. The enzymes that regulate
levels of histone acetylation are histone acetyltransferases (HATs),
which activate gene expression and histone deacetylases (HDACs), that
repress gene expression. Acetylation together with other histone and DNA
modifications regulate transcription profiles for specific cellular
functions. Our previous research has demonstrated a pivotal role for
cyclicAMP response element binding protein (CREB)-binding protein (CBP),
a histone acetyltransferase, in long-term memory for novel object
recognition (NOR). In fact, every genetically modifiedCbp mutant mouse
characterized thus far exhibits impaired long-term memory for NOR. These
results suggest that long-term memory for NOR is especially sensitive to
alterations in CBP activity. Thus, in the current study, we examined the
role of HDACs in memory for NOR. We found that inducing a histone
hyperacetylated state via HDAC inhibition transforms a learning event
that would not normally result in long-term memory into an event that is
now remembered long-term. We have also found that HDAC inhibition
generates a type of long-term memory that persists beyond a point at
which normal memory for NOR fails. This result is particularly
interesting because one alluring aspect of examining the role of
chromatin modifications in modulating transcription required for
long-term memory processes is that these modifications may provide
potentially stable epigenetic markers in the service of activating
and/or maintaining transcriptional processes.
Publication Types:
* Research Support, N.I.H., Extramural
* Research Support, Non-U.S. Gov't
PMID: 19470462 |
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