CPEB

<h2 id="protein-family">Protein Family</h2>
CPEB can also refer to the family of proteins.<a class="footnote-ref" id="fnref:18" href="#fn:18">18</a> There are four proteins in the protein family:

<ul><li><a href="/facts/CPEB1/aRxXAxa1">CPEB1</a></li>
<li>CPEB2</li>
<li>CPEB3</li>
<li>CPEB4</li></ul>
This protein family can be divided into two subfamilies. The groups are separated by their<a class="footnote-ref" id="fnref:19" href="#fn:19">19</a> ..specific properties in target/motif recognition, large-order complex co-factors, and dynamic properties and regulation during cell cycle."<a class="footnote-ref" id="fnref:20" href="#fn:20">20</a> The first subfamily contains only CPEB1 and the second contains CPEB2 - CPEB4. The general CPE that CPEBs bind to has a canonical UUUUAU sequence, which all four of the proteins can recognize. However, CPEB1 can only recognize CPEs with the canonical sequence, while the second group of CPEB2–4 can also bind to variants of the CPE, known as G-variants due to their sequence difference (UUUUGU). This suggests that CPEB2–4 has other targets that it can hit in addition to CPEB1 targets.

<h2 id="structure">Structure</h2>
The CPEB structure consists of "...an <a href="/facts/Amino-terminal/yKYpuaBJ">amino-terminal</a> port<a class="footnote-ref" id="fnref:21" href="#fn:21">21</a> with no obvious functional motif, two <a href="/facts/RNA_recognition_motif/eDoIa4tb">RNA recognition motifs</a> (RRMS), and a cysteine-histidine region that is reminiscent of a zinc finger."<a class="footnote-ref" id="fnref:22" href="#fn:22">22</a> The zinc finger region and RRMs are necessary for RNA bind.<a class="footnote-ref" id="fnref:23" href="#fn:23">23</a> It was found that CPEB bound to other metals than zinc destroyed RNA binding, but the binding would be restored if supplemented with zinc.<a class="footnote-ref" id="fnref:24" href="#fn:24">24</a> Proteins lacking any of the RRMs were also shown to be less efficient in binding RNA.
Not all of the regions are the same across the different forms of CPEB. The amino terminus can differ substantially across the proteins. The prion-like isoform of CPEB found in Aplysia californica, Drosophila, mice, and humans is an example of such differentiation.<a class="footnote-ref" id="fnref:25" href="#fn:25">25</a> This isoform is prion-like due to the presence of polyglutamine- or polyalanine-rich domains at the N-terminus.<a class="footnote-ref" id="fnref:26" href="#fn:26">26</a>

<h2 id="neurological-disorders">Neurological disorders</h2>
A misstep in the process of translation with CPEB can lead to possible adverse affects on neurological development. Risk genes for <a href="/facts/Autism_spectrum/bzouRyMI">autism spectrum disorder</a> were found in brains where "...CPEB4 transcript isoform imbalance due to decreased inclusion of a neuronal-specific microexon together with a new molecular signature of global polyadenine tail shortening..."<a class="footnote-ref" id="fnref:27" href="#fn:27">27</a> In idiopathic autism spectrum disorder individuals, CPEB4 is greatly decreased and showed significant splicing alterations. An equivalent isoform imbalance in mice mimics changes of autism spectrum disorder genes, which causes similar neuroanatomical, electrophysiological, and behavioral phenotype expression.
Gene regulation of CPEB proteins is also proposed as a target for gene therapy..<a class="footnote-ref" id="fnref:28" href="#fn:28">28</a> <a href="/facts/Fragile_X_syndrome/WWjbEWQE">Fragile X syndrome</a> and <a href="/facts/Huntington%27s_disease/2P6yCoeK">Huntington's disease</a> are two such disorders and diseases where CPEB regulation has been used to attempt recovery of brain function. There is not a cure for either of these afflictions, but translation dysfunction of CPEB proteins can be a cause for either.<a class="footnote-ref" id="fnref:29" href="#fn:29">29</a> When modeling fragile X syndrome in mice, CPEB1 gene mutations reduced pathological processes associated with the disorder.<a class="footnote-ref" id="fnref:30" href="#fn:30">30</a> A decrease in CPEB1 restored the balance of mRNA translation, which can be achieved by manipulating levels of miRNAs.
For Huntington's disease, a study on a Drosophila cell culture showed that the Drosophila Orb2A protein was absorbed on the surface of <a href="/facts/Huntingtin/fYK4y480">Huntingtin gene (Htt)</a> aggregates.<a class="footnote-ref" id="fnref:31" href="#fn:31">31</a> The aggregates lead to a protein synthesis imbalance, cell decay, and neuron death. The absorption of the protein caused a partial reduction of the lethality of the Htt aggregates. The aggregates did not decrease, but protein synthesis balance was restored in the cells. However, CPEB sequestration translation dysfunction is not a definite cause of Huntington's disease symptoms in humans. Other RNA binding proteins could be other possible targets for translation dysfunction in patients with this disease.

<h2 id="role-in-cellular-senescence">Role in cellular senescence</h2>
CPEB has been found to help regulate <a href="/facts/Cellular_senescence/w6f0gfrB">cellular senescence</a> through modulating <a href="/facts/P53/YEGULLgM">p53</a> mRNA polyadenylation-induced translation.<a class="footnote-ref" id="fnref:32" href="#fn:32">32</a> When human skin and lung cells were put under a knockdown of CPEB, they bypassed the M1 crisis stage of senescence. This bypass is required for cellular transformation. Reduced CPEB levels also affected the rate at which cell division occurred, slowing down the process until the cells ceased to divide. In mice, reduced CPEB levels caused cells to become immortal.<a class="footnote-ref" id="fnref:33" href="#fn:33">33</a> A senescence-like phenotype recurred when CPEB was introduced into early passage cells, but not late passage cells. Senescence is considered an irreversible process, but the CPEB-induced senescence-like phenotype can possibly refute that. CPEB is thus shown to regulate senescence, as well as mediate immortalization in cells.

<h2 id="role-in-memory">Role in memory</h2>
Drosophila Orb2 binds to genes implicated in long-term memory. An isoform of CPEB found in the <a href="/facts/Neuron/G7CyTVdH">neurons</a> of the sea slug <a href="/facts/Aplysia_californica/ktDqILVX">Aplysia californica</a>, as well as in <a href="/facts/Drosophila/P4K7RkJl">Drosophila</a>, mice, and humans, contains an <a href="/facts/N-terminus/yKYpuaBJ">N-terminal</a> domain not found in other isoforms that shows high sequence similarity to <a href="/facts/Prion/UJfG9EfS">prion</a> proteins. Experiments with the Aplysia isoform expressed in <a href="/facts/Yeast/eGD24nfI">yeast</a> reveal that CPEB has a key property associated with prions: it can cause other proteins to assume alternate <a href="/facts/Tertiary_structure/VaN6MEYh">protein conformations</a> that are <a href="/facts/Heritable/t0aMmRWx">heritable</a> in successive generations of yeast cells. Furthermore, the functional RNA-binding form of the CPEB protein may be the prion-like state.<a class="footnote-ref" id="fnref:34" href="#fn:34">34</a> These observations have led to the suggestion that long-lasting bistable prionlike proteins play a role in the formation of long-term <a href="/facts/Memory/zucwQIEX">memory</a>.<a class="footnote-ref" id="fnref:35" href="#fn:35">35</a>
It has been suggested that "both memory storage and its underlying synaptic plasticity are mediated by the increase in. . .CPEB."<a class="footnote-ref" id="fnref:36" href="#fn:36">36</a>

<h2 id="role-in-oogenesis-and-embryonic-development">Role in oogenesis and embryonic development</h2>
CPEBs are responsible for the polyadenine tail length in oocytes during <a href="/facts/Oogenesis/4yHrJAwe">oogenesis</a>. In Xenopus and mice oocytes, CPEB has been noted to control oocyte growth. Regulation of follicle development has been noted specifically in mice.<a class="footnote-ref" id="fnref:37" href="#fn:37">37</a> CPEB regulates oocyte development and follicle development in the <a href="/facts/Dictyate/AC9neESR">dictyate</a> stage through phosphorylation and dephosphorylation.<a class="footnote-ref" id="fnref:38" href="#fn:38">38</a> During <a href="/facts/Pachytene/Pj5Q6nGN">pachytene</a>, CPEB is phosphorylated, which controls polyadenylation and translation of mRNAs.<a class="footnote-ref" id="fnref:39" href="#fn:39">39</a> An experiment was conducted to determine how CPEB affected development by inhibiting the protein in mice. It was found that CPEB regulates <a href="/facts/Growth_differentiation_factor-9/VAuwGwxs">Gdf9</a>, a growth factor necessary for follicle development. Without CPEB, Gdf9 had a shortened polyadenine tail and reduced expression. It was also found that progressive oocyte loss and infertility arose from the knockdown of CPEB in oocytes, which resembles <a href="/facts/Premature_ovarian_failure/X3GjNkBN">premature ovarian failure</a> syndrome in humans.<a class="footnote-ref" id="fnref:40" href="#fn:40">40</a>

<h2 id="interactions">Interactions</h2>
CPEB has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with the following proteins:

<ul><li><a href="/facts/PUM2/n3f5H19Q">PUM2</a><a class="footnote-ref" id="fnref:41" href="#fn:41">41</a></li>
<li><a href="/facts/PARN/RpzNR2JI">PARN</a><a class="footnote-ref" id="fnref:42" href="#fn:42">42</a></li>
<li><a href="/facts/GLD-2/WGMlIUcD">GLD-2</a><a class="footnote-ref" id="fnref:43" href="#fn:43">43</a></li>
<li><a href="/facts/SYMPK/64qsAvGz">symplekin</a><a class="footnote-ref" id="fnref:44" href="#fn:44">44</a></li>
<li><a href="/facts/EIF4EBP1/PG71HBXI">eIF4E binding protein</a><a class="footnote-ref" id="fnref:45" href="#fn:45">45</a></li></ul>

<h2 id="references">References</h2>

<ol>
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<li id="fn:14">Lin CL, Evans V, Shen S, Xing Y, Richter JD (February 2010). "The nuclear experience of CPEB: implications for RNA processing and translational control". RNA. 16 (2): 338–348. doi:10.1261/rna.1779810. PMC 2811663. PMID 20040591. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811663" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811663</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></li>
<li id="fn:15">Hake LE, Richter JD (November 1994). "CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation". Cell. 79 (4): 617–627. doi:10.1016/0092-8674(94)90547-9. PMID 7954828. S2CID 42910508. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></li>
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<li id="fn:21">Hake LE, Mendez R, Richter JD (February 1998). "Specificity of RNA binding by CPEB: requirement for RNA recognition motifs and a novel zinc finger". Molecular and Cellular Biology. 18 (2): 685–693. doi:10.1128/MCB.18.2.685. PMC 108779. PMID 9447964. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779</a> <a href="#fnref:21" class="footnote-back-ref">↩</a></li>
<li id="fn:22">Hake LE, Mendez R, Richter JD (February 1998). "Specificity of RNA binding by CPEB: requirement for RNA recognition motifs and a novel zinc finger". Molecular and Cellular Biology. 18 (2): 685–693. doi:10.1128/MCB.18.2.685. PMC 108779. PMID 9447964. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779</a> <a href="#fnref:22" class="footnote-back-ref">↩</a></li>
<li id="fn:23">Hake LE, Mendez R, Richter JD (February 1998). "Specificity of RNA binding by CPEB: requirement for RNA recognition motifs and a novel zinc finger". Molecular and Cellular Biology. 18 (2): 685–693. doi:10.1128/MCB.18.2.685. PMC 108779. PMID 9447964. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779</a> <a href="#fnref:23" class="footnote-back-ref">↩</a></li>
<li id="fn:24">Hake LE, Mendez R, Richter JD (February 1998). "Specificity of RNA binding by CPEB: requirement for RNA recognition motifs and a novel zinc finger". Molecular and Cellular Biology. 18 (2): 685–693. doi:10.1128/MCB.18.2.685. PMC 108779. PMID 9447964. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108779</a> <a href="#fnref:24" class="footnote-back-ref">↩</a></li>
<li id="fn:25">Kozlov E, Shidlovskii YV, Gilmutdinov R, Schedl P, Zhukova M (March 2021). "The role of CPEB family proteins in the nervous system function in the norm and pathology". Cell & Bioscience. 11 (1): 64. doi:10.1186/s13578-021-00577-6. PMC 8011179. PMID 33789753. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011179" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011179</a> <a href="#fnref:25" class="footnote-back-ref">↩</a></li>
<li id="fn:26">Kozlov E, Shidlovskii YV, Gilmutdinov R, Schedl P, Zhukova M (March 2021). "The role of CPEB family proteins in the nervous system function in the norm and pathology". Cell & Bioscience. 11 (1): 64. doi:10.1186/s13578-021-00577-6. PMC 8011179. PMID 33789753. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011179" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011179</a> <a href="#fnref:26" class="footnote-back-ref">↩</a></li>
<li id="fn:27">Parras A, Anta H, Santos-Galindo M, Swarup V, Elorza A, Nieto-González JL, et al. (August 2018). "Autism-like phenotype and risk gene mRNA deadenylation by CPEB4 mis-splicing". Nature. 560 (7719): 441–446. Bibcode:2018Natur.560..441P. doi:10.1038/s41586-018-0423-5. PMC 6217926. PMID 30111840. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6217926" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6217926</a> <a href="#fnref:27" class="footnote-back-ref">↩</a></li>
<li id="fn:28">Kozlov E, Shidlovskii YV, Gilmutdinov R, Schedl P, Zhukova M (March 2021). "The role of CPEB family proteins in the nervous system function in the norm and pathology". Cell & Bioscience. 11 (1): 64. doi:10.1186/s13578-021-00577-6. PMC 8011179. PMID 33789753. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011179" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8011179</a> <a href="#fnref:28" class="footnote-back-ref">↩</a></li>
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<li id="fn:30">Udagawa T, Farny NG, Jakovcevski M, Kaphzan H, Alarcon JM, Anilkumar S, et al. (November 2013). "Genetic and acute CPEB1 depletion ameliorate fragile X pathophysiology". Nature Medicine. 19 (11): 1473–1477. doi:10.1038/nm.3353. PMC 3823751. PMID 24141422. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823751" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823751</a> <a href="#fnref:30" class="footnote-back-ref">↩</a></li>
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</ol>

CPEB open-in-new

CPEB