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RBBP4
open-in-new
<h2 id="function">Function</h2> <p>This gene encodes a ubiquitously expressed nuclear protein that belongs to a highly conserved subfamily of <a href="/facts/WD40_repeat/0DxvU1fg">WD-repeat</a> proteins. It is present in protein complexes involved in <a href="/facts/Histone_acetylation_and_deacetylation/jafcW82T">histone acetylation</a> and <a href="/facts/Chromatin/ha0TJheJ">chromatin</a> assembly. It is part of the <a href="/facts/Mi-2%2fNuRD_complex/gY2Vly2Y">Mi-2/NuRD complex</a> that has been implicated in <a href="/facts/Chromatin_remodeling/ukC9TjoG">chromatin remodeling</a> and transcriptional repression associated with histone deacetylation. This encoded protein is also part of <a href="/facts/Corepressor/2C1GqzD0">corepressor</a> complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to <a href="/facts/Retinoblastoma_protein/qc2WKTc4">retinoblastoma protein</a> to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of <a href="/facts/E2F/18zluKwA">E2F</a>-responsive genes.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> </p> <h2 id="clinical-significance">Clinical significance</h2> <p>A decrease of RbAp48 in the <a href="/facts/Dentate_gyrus/S8a0mopL">dentate gyrus</a> (DG) of the <a href="/facts/Hippocampus/X7CqbP8X">hippocampus</a> in the <a href="/facts/Brain/EKla9NkJ">brain</a> is suspected to be a main cause of <a href="/facts/Memory_loss/PaMeGJH7">memory loss</a> in normal <a href="/facts/Aging/AxL4qCW4">aging</a>.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> An age related decrease in RbAp48 is observed in the DG from human post-mortem tissue and also in mice. Furthermore, a <a href="/facts/Gene_knockin/khSPPo1d">gene knockin</a> of a <a href="/facts/Dominant_negative/0VyT59Sg">dominant negative</a> form of RbAp48 of causes memory deficits in young mice similar to that observed in older mice. Using <a href="/facts/Lentivirus/ThuASV8M">lentiviral gene transfer</a> to increase the expression of RbAp48 in the brain reverses memory deficits in older mice.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> </p><p>RBBP4 works at least in part through the <a href="/facts/Protein_kinase_A/kaKoYfbp">PKA</a>-<a href="/facts/CREB1/l1aGTdNA">CREB1</a>-<a href="/facts/CREB-binding_protein/F4p9VIV7">CPB</a> pathway.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> Hence one possible therapeutic approach to restore age-related memory loss is the use of PKA-CREB1-CPB pathway stimulating drugs. It has previously been shown that dopamine D1/D5 agonists such as <a href="/facts/6-Br-APB/Us1KXAbv">6-Br-APB</a> and <a href="/facts/SKF-38%2c393/DCfF9m51">SKF-38,393</a> that are positively coupled to <a href="/facts/Adenylyl_cyclase/WnCSuV96">adenylyl cyclase</a> and the <a href="/facts/3%2527%2c5%2527-cyclic-AMP_phosphodiesterase/6nbp5wz2">cAMP phosphodieserase</a> inhibitor <a href="/facts/Rolipram/RwpMRbpt">rolipram</a> reduce memory defects in aged mice.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>RBBP4 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/BRCA1/xHDwxARA">BRCA1</a>,<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a></li> <li><a href="/facts/CREB-binding_protein/F4p9VIV7">CREBBP</a>,<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a></li> <li><a href="/facts/GATAD2B/kLlpzqeX">GATAD2B</a>,<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a></li> <li><a href="/facts/HDAC1/6Ah3cBy1">HDAC1</a>,<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a><a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a><a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a><a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a><a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a><a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a><a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a><a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a></li> <li><a href="/facts/Histone_deacetylase_2/FRWRaCRL">HDAC2</a>,<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a><a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a><a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a></li> <li><a href="/facts/HDAC3/lewe7kpB">HDAC3</a>,<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a></li> <li><a href="/facts/MTA2/63kybTVf">MTA2</a>,<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a><a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a></li> <li><a href="/facts/Retinoblastoma_protein/qc2WKTc4">RB</a>,<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a><a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a><a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a></li> <li><a href="/facts/SAP30/9Y758sYv">SAP30</a>,<a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a><a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a><a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a> and</li> <li><a href="/facts/SIN3A/AVoVVgV6">SIN3A</a>.<a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a><a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li><a href="https://www.ncbi.nlm.nih.gov/gene/5928">"RBBP4 retinoblastoma binding protein 4 [Homo sapiens (human)]"</a>. Bethesda, MD: <a href="/facts/National_Center_for_Biotechnology_Information/6Xj5wCbu">National Center for Biotechnology Information (NCBI)</a>. Retrieved 2013-09-06.</li> <li>Bauw G, Rasmussen HH, van den Bulcke M, et al. (1990). "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes". <i>Electrophoresis</i>. 11 (7): 528–36. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Felps.1150110703">10.1002/elps.1150110703</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1699755">1699755</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:24768114">24768114</a>.</li> <li>Grozinger CM, Hassig CA, Schreiber SL (1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21783">"Three proteins define a class of human histone deacetylases related to yeast Hda1p"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 96 (9): 4868–73. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1999PNAS...96.4868G">1999PNAS...96.4868G</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.96.9.4868">10.1073/pnas.96.9.4868</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21783">21783</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10220385">10220385</a>.</li> <li>Hassig CA, Tong JK, Fleischer TC, et al. (1998). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC19868">"A role for histone deacetylase activity in HDAC1-mediated transcriptional repression"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 95 (7): 3519–24. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998PNAS...95.3519H">1998PNAS...95.3519H</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.95.7.3519">10.1073/pnas.95.7.3519</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC19868">19868</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9520398">9520398</a>.</li> <li>Marheineke K, Krude T (1998). <a href="https://doi.org/10.1074%2Fjbc.273.24.15279">"Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle"</a>. <i>J. Biol. Chem</i>. 273 (24): 15279–86. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.24.15279">10.1074/jbc.273.24.15279</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9614144">9614144</a>.</li> <li>Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". <i>Gene</i>. 138 (1–2): 171–4. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0378-1119%2894%2990802-8">10.1016/0378-1119(94)90802-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8125298">8125298</a>.</li> <li>Qian YW, Lee EY (1995). <a href="https://doi.org/10.1074%2Fjbc.270.43.25507">"Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast"</a>. <i>J. Biol. Chem</i>. 270 (43): 25507–13. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.270.43.25507">10.1074/jbc.270.43.25507</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7503932">7503932</a>.</li> <li>Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". <i>Electrophoresis</i>. 13 (12): 960–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Felps.11501301199">10.1002/elps.11501301199</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/1286667">1286667</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:41855774">41855774</a>.</li> <li>Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". <i>Gene</i>. 200 (1–2): 149–56. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0378-1119%2897%2900411-3">10.1016/S0378-1119(97)00411-3</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9373149">9373149</a>.</li> <li>Taunton J, Hassig CA, Schreiber SL (1996). "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p". <i>Science</i>. 272 (5260): 408–11. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1996Sci...272..408T">1996Sci...272..408T</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.272.5260.408">10.1126/science.272.5260.408</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8602529">8602529</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:25717734">25717734</a>.</li> <li>Tong JK, Hassig CA, Schnitzler GR, et al. (1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". <i>Nature</i>. 395 (6705): 917–21. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998Natur.395..917T">1998Natur.395..917T</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F27699">10.1038/27699</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9804427">9804427</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4355885">4355885</a>.</li> <li>Verreault A, Kaufman PD, Kobayashi R, Stillman B (1998). <a href="https://doi.org/10.1016%2FS0960-9822%2898%2970040-5">"Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase"</a>. <i>Curr. Biol</i>. 8 (2): 96–108. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998CBio....8...96V">1998CBio....8...96V</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0960-9822%2898%2970040-5">10.1016/S0960-9822(98)70040-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9427644">9427644</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:201273">201273</a>.</li> <li>Verreault A, Kaufman PD, Kobayashi R, Stillman B (1996). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2981326-4">"Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4"</a>. <i>Cell</i>. 87 (1): 95–104. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2981326-4">10.1016/S0092-8674(00)81326-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8858152">8858152</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:1416453">1416453</a>.</li> <li>Wolffe AP, Urnov FD, Guschin D (2001). "Co-repressor complexes and remodelling chromatin for repression". <i>Biochem. Soc. Trans</i>. 28 (4): 379–86. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1042%2F0300-5127%3A0280379">10.1042/0300-5127:0280379</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10961924">10961924</a>.</li> <li>Yarden RI, Brody LC (1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21803">"BRCA1 interacts with components of the histone deacetylase complex"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 96 (9): 4983–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1999PNAS...96.4983Y">1999PNAS...96.4983Y</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.96.9.4983">10.1073/pnas.96.9.4983</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21803">21803</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10220405">10220405</a>.</li> <li>Zhang Y, Ng HH, Erdjument-Bromage H, et al. (1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316920">"Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation"</a>. <i>Genes Dev</i>. 13 (15): 1924–35. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgad.13.15.1924">10.1101/gad.13.15.1924</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316920">316920</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10444591">10444591</a>.</li> <li>Zhang Y, Iratni R, Erdjument-Bromage H, et al. (1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980216-0">"Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex"</a>. <i>Cell</i>. 89 (3): 357–64. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980216-0">10.1016/S0092-8674(00)80216-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9150135">9150135</a>.</li> <li>Zhang Y, Sun ZW, Iratni R, et al. (1998). <a href="https://doi.org/10.1016%2FS1097-2765%2800%2980102-1">"SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex"</a>. <i>Mol. Cell</i>. 1 (7): 1021–31. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS1097-2765%2800%2980102-1">10.1016/S1097-2765(00)80102-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9651585">9651585</a>.</li> <li>Zhang Y, LeRoy G, Seelig HP, et al. (1998). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2981758-4">"The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities"</a>. <i>Cell</i>. 95 (2): 279–89. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2981758-4">10.1016/S0092-8674(00)81758-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9790534">9790534</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:18786866">18786866</a>.</li> <li>Zhang Y, Dufau ML (2003). <a href="https://zenodo.org/record/1260176">"Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes"</a>. <i>J. Steroid Biochem. Mol. 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