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@ARTICLE{Turimella:141160,
author = {Turimella, Sada Lakshmi and Bedner, Peter and Skubal,
Magdalena and Vangoor, Vamshidhar Reddy and Kaczmarczyk,
Lech and Karl, Kevin and Zoidl, Georg and Gieselmann,
Volkmar and Seifert, Gerald and Steinhäuser, Christian and
Kandel, Eric and Theis, Martin},
title = {{C}haracterization of cytoplasmic polyadenylation element
binding 2 protein expression and its {RNA} binding
activity.},
journal = {Hippocampus},
volume = {25},
number = {5},
issn = {1050-9631},
address = {New York, NY [u.a.]},
publisher = {Wiley},
reportid = {DZNE-2020-07482},
pages = {630-642},
year = {2015},
abstract = {Cytoplasmic polyadenylation element binding (CPEB) proteins
are translational regulators that are involved in the
control of cellular senescence, synaptic plasticity,
learning, and memory. We have previously found all four
known CPEB family members to be transcribed in the mouse
hippocampus. Aside from a brief description of CPEB2 in
mouse brain, not much is known about its biological role.
Hence, this study aims to investigate CPEB2 expression in
mouse brain. With reverse transcription polymerase chain
reaction (RT-PCR) of total mouse brain cDNA, we identified
four distinct CPEB2 splice variants. Single-cell RT-PCR
showed that CPEB2 is predominantly expressed in neurons of
the juvenile and adult brain and that individual cells
express different sets of splice variants. Staining of brain
slices with a custom-made CPEB2 antibody revealed ubiquitous
expression of the protein in many brain regions, including
hippocampus, striatum, thalamus, cortex, and cerebellum. We
also found differential expression of CPEB2 protein in
excitatory, inhibitory, and dopaminergic neurons. In primary
hippocampal cultures, the subcellular localization of CPEB2
in neurons and astrocytes resembled that of CPEB1.
Electrophoretic mobility shift assay and RNA
coimmunoprecipitation revealed CPEB2 interaction with
β-catenin and Ca(2+) /calmodulin-dependent protein kinase
II (both established CPEB1 targets), indicating an overlap
in RNA binding specificity between CPEB1 and CPEB2.
Furthermore, we identified ephrin receptor A4 as a putative
novel target of CPEB2. In conclusion, our study identifies
CPEB2 splice variants to be differentially expressed among
individual cells and across cell types of the mouse
hippocampus, and reveals overlapping binding specificity
between CPEB2 and CPEB1.},
keywords = {Animals / Astrocytes: metabolism / Brain: growth $\&$
development / Brain: metabolism /
Calcium-Calmodulin-Dependent Protein Kinase Type 2:
metabolism / HeLa Cells / Humans / Mice / Neurons:
metabolism / Protein Isoforms / RNA: metabolism / RNA,
Messenger: metabolism / RNA-Binding Proteins: genetics /
RNA-Binding Proteins: metabolism / Receptor, EphA4:
metabolism / Transcription Factors: genetics / Transcription
Factors: metabolism / Transfection / beta Catenin:
metabolism / mRNA Cleavage and Polyadenylation Factors:
genetics / mRNA Cleavage and Polyadenylation Factors:
metabolism / CPEB2 protein, mouse (NLM Chemicals) / Cpeb1
protein, mouse (NLM Chemicals) / Protein Isoforms (NLM
Chemicals) / RNA, Messenger (NLM Chemicals) / RNA-Binding
Proteins (NLM Chemicals) / Transcription Factors (NLM
Chemicals) / beta Catenin (NLM Chemicals) / mRNA Cleavage
and Polyadenylation Factors (NLM Chemicals) / RNA (NLM
Chemicals) / Receptor, EphA4 (NLM Chemicals) /
Calcium-Calmodulin-Dependent Protein Kinase Type 2 (NLM
Chemicals)},
cin = {AG Jackson},
ddc = {610},
cid = {I:(DE-2719)1013019},
pnm = {342 - Disease Mechanisms and Model Systems (POF3-342)},
pid = {G:(DE-HGF)POF3-342},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:25483308},
doi = {10.1002/hipo.22399},
url = {https://pub.dzne.de/record/141160},
}