# RBBP4

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{{Short description|Protein-coding gene in the species Homo sapiens}}
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{{Infobox_gene}}
'''Histone-binding protein RBBP4''' (also known as '''RbAp48''', or '''NURF55''') is a [protein](/source/protein) that in humans is encoded by the ''RBBP4'' [gene](/source/gene).<ref name="pmid8350924">{{cite journal |vauthors=Qian YW, Wang YC, Hollingsworth RE Jr, Jones D, Ling N, Lee EY | title = A retinoblastoma-binding protein related to a negative regulator of Ras in yeast | journal = Nature | volume = 364 | issue = 6438 | pages = 648–52 |date=September 1993 | pmid = 8350924 | doi = 10.1038/364648a0 | bibcode = 1993Natur.364..648Q | s2cid = 4303062 }}</ref><ref name="pmid14609955">{{cite journal |vauthors=Barak O, Lazzaro MA, Lane WS, Speicher DW, Picketts DJ, Shiekhattar R | title = Isolation of human NURF: a regulator of Engrailed gene expression | journal = EMBO J | volume = 22 | issue = 22 | pages = 6089–100 |date=November 2003 | pmid = 14609955 | pmc = 275440 | doi = 10.1093/emboj/cdg582 }}</ref>

== Function ==
This gene encodes a ubiquitously expressed nuclear protein that belongs to a highly conserved subfamily of [WD-repeat](/source/WD40_repeat) proteins. It is present in protein complexes involved in [histone acetylation](/source/histone_acetylation_and_deacetylation) and [chromatin](/source/chromatin) assembly. It is part of the [Mi-2/NuRD complex](/source/Mi-2%2FNuRD_complex) that has been implicated in [chromatin remodeling](/source/chromatin_remodeling) and transcriptional repression associated with [histone deacetylation](/source/histone_deacetylation). This encoded protein is also part of [corepressor](/source/corepressor) complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to [retinoblastoma protein](/source/retinoblastoma_protein) to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of [E2F](/source/E2F)-responsive genes.<ref name="entrez">{{cite web | title = Entrez Gene: RBBP4 retinoblastoma-binding protein 4| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5928}}</ref>

== Clinical significance ==
A decrease of RbAp48 in the [dentate gyrus](/source/dentate_gyrus) (DG) of the [hippocampus](/source/hippocampus) in the [brain](/source/brain) is suspected to be a main cause of [memory loss](/source/memory_loss) in normal [aging](/source/aging).<ref name="Pavlopoulos_2013">{{cite journal |vauthors=Pavlopoulos E, Jones S, Kosmidis S, Close M, Kim C, Kovalerchik O, Small SA, Kandel ER | title = Molecular Mechanism for Age-Related Memory Loss: The Histone-Binding Protein RbAp48 | journal = Sci Transl Med | volume = 5 | issue = 200 | pages = 200ra115 |date=August 2013 | pmid = 23986399 | doi = 10.1126/scitranslmed.3006373 | pmc=4940031}}</ref>  An age related decrease in RbAp48 is observed in the DG from human post-mortem tissue and also in mice.  Furthermore, a [gene knockin](/source/gene_knockin) of a [dominant negative](/source/dominant_negative) form of RbAp48 causes memory deficits in young mice similar to that observed in older mice. Using [lentiviral gene transfer](/source/Lentivirus) to increase the expression of RbAp48 in the brain reverses memory deficits in older mice.<ref name="Pavlopoulos_2013"/>

RBBP4 works at least in part through the [PKA](/source/Protein_kinase_A)-[CREB1](/source/CREB1)-[CPB](/source/CREB-binding_protein) pathway.<ref name="Pavlopoulos_2013"/> 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 [6-Br-APB](/source/6-Br-APB) and [SKF-38,393](/source/SKF-38%2C393) that are positively coupled to [adenylyl cyclase](/source/adenylyl_cyclase) and the [cAMP phosphodieserase](/source/3'%2C5'-cyclic-AMP_phosphodiesterase) inhibitor [rolipram](/source/rolipram) reduce memory defects in aged mice.<ref name="pmid10220457">{{cite journal |vauthors=Bach ME, Barad M, Son H, Zhuo M, Lu YF, Shih R, Mansuy I, Hawkins RD, Kandel ER | title = Age-related defects in spatial memory are correlated with defects in the late phase of hippocampal long-term potentiation in vitro and are attenuated by drugs that enhance the cAMP signaling pathway | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 9 | pages = 5280–5 |date=April 1999 | pmid = 10220457 | pmc = 21855 | doi = 10.1073/pnas.96.9.5280| bibcode = 1999PNAS...96.5280B | doi-access = free }}</ref>

==Interactions==
RBBP4 has been shown to [interact](/source/Protein-protein_interaction) with:
* [BRCA1](/source/BRCA1),<ref name = pmid10220405>{{cite journal |vauthors=Yarden RI, Brody LC | title = BRCA1 interacts with components of the histone deacetylase complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 9 | pages = 4983–8 | year = 1999 | pmid = 10220405 | pmc = 21803 | doi = 10.1073/pnas.96.9.4983| bibcode = 1999PNAS...96.4983Y | doi-access = free }}</ref>
* [CREBBP](/source/CREB-binding_protein),<ref name = pmid10866654>{{cite journal |vauthors=Zhang Q, Vo N, Goodman RH | title = Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB | journal = Mol. Cell. Biol. | volume = 20 | issue = 14 | pages = 4970–8 | year = 2000 | pmid = 10866654 | pmc = 85947 | doi = 10.1128/MCB.20.14.4970-4978.2000}}</ref>
* [GATAD2B](/source/GATAD2B),<ref name = pmid11756549>{{cite journal |vauthors=Feng Q, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Zhang Y | title = Identification and functional characterization of the p66/p68 components of the MeCP1 complex | journal = Mol. Cell. Biol. | volume = 22 | issue = 2 | pages = 536–46 | year = 2002 | pmid = 11756549 | pmc = 139742 | doi = 10.1128/MCB.22.2.536-546.2002}}</ref>
* [HDAC1](/source/HDAC1),<ref name = pmid12943729>{{cite journal |vauthors=Zhang Y, Dufau ML | title = Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes | journal = J. Steroid Biochem. Mol. Biol. | volume = 85 | issue = 2–5 | pages = 401–14 | year = 2003 | pmid = 12943729 | doi = 10.1016/S0960-0760(03)00230-9| s2cid = 28512341 | url = https://zenodo.org/record/1260176 }}</ref><ref name = pmid12920132>{{cite journal |vauthors=Yao YL, Yang WM | title = The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity | journal = J. Biol. Chem. | volume = 278 | issue = 43 | pages = 42560–8 | year = 2003 | pmid = 12920132 | doi = 10.1074/jbc.M302955200 | doi-access = free }}</ref><ref name = pmid11470869>{{cite journal |vauthors=Nicolas E, Ait-Si-Ali S, Trouche D | title = The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein | journal = Nucleic Acids Res. | volume = 29 | issue = 15 | pages = 3131–6 | year = 2001 | pmid = 11470869 | pmc = 55834 | doi = 10.1093/nar/29.15.3131}}</ref><ref name = pmid10220385>{{cite journal |vauthors=Grozinger CM, Hassig CA, Schreiber SL | title = Three proteins define a class of human histone deacetylases related to yeast Hda1p | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 9 | pages = 4868–73 | year = 1999 | pmid = 10220385 | pmc = 21783 | doi = 10.1073/pnas.96.9.4868| bibcode = 1999PNAS...96.4868G | doi-access = free }}</ref><ref name = pmid11171972>{{cite journal |vauthors=You A, Tong JK, Grozinger CM, Schreiber SL | title = CoREST is an integral component of the CoREST- human histone deacetylase complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 4 | pages = 1454–8 | year = 2001 | pmid = 11171972 | pmc = 29278 | doi = 10.1073/pnas.98.4.1454 | bibcode = 2001PNAS...98.1454Y | doi-access = free }}</ref><ref name = pmid9150133>{{cite journal |vauthors=Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE | title = Histone deacetylase activity is required for full transcriptional repression by mSin3A | journal = Cell | volume = 89 | issue = 3 | pages = 341–7 | year = 1997 | pmid = 9150133 | doi = 10.1016/S0092-8674(00)80214-7| s2cid = 14233219 | doi-access = free }}</ref><ref name = pmid10471499>{{cite journal |vauthors=Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A | title = MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex | journal = Nat. Genet. | volume = 23 | issue = 1 | pages = 58–61 | year = 1999 | pmid = 10471499 | doi = 10.1038/12659 | hdl = 1842/684 | s2cid = 6147725 | hdl-access = free }}</ref><ref name = pmid10444591>{{cite journal |vauthors=Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D | title = Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation | journal = Genes Dev. | volume = 13 | issue = 15 | pages = 1924–35 | year = 1999 | pmid = 10444591 | pmc = 316920 | doi = 10.1101/gad.13.15.1924}}</ref><ref name = pmid12091390>{{cite journal |vauthors=Zhang Y, Dufau ML | title = Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex | journal = J. Biol. Chem. | volume = 277 | issue = 36 | pages = 33431–8 | year = 2002 | pmid = 12091390 | doi = 10.1074/jbc.M204417200 | doi-access = free }}</ref><ref name = pmid9520398>{{cite journal |vauthors=Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL | title = A role for histone deacetylase activity in HDAC1-mediated transcriptional repression | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 7 | pages = 3519–24 | year = 1998 | pmid = 9520398 | pmc = 19868 | doi = 10.1073/pnas.95.7.3519| bibcode = 1998PNAS...95.3519H | doi-access = free }}</ref><ref name = pmid9150135>{{cite journal |vauthors=Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D | title = Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex | journal = Cell | volume = 89 | issue = 3 | pages = 357–64 | year = 1997 | pmid = 9150135 | doi = 10.1016/S0092-8674(00)80216-0| doi-access = free }}</ref>
* [HDAC2](/source/Histone_deacetylase_2),<ref name = pmid12943729/><ref name = pmid12091390/><ref name = pmid12493763>{{cite journal |vauthors=Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R | title = A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes | journal = J. Biol. Chem. | volume = 278 | issue = 9 | pages = 7234–9 | year = 2003 | pmid = 12493763 | doi = 10.1074/jbc.M208992200 | doi-access = free }}</ref><ref name = pmid9804427>{{cite journal |vauthors=Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL | title = Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex | journal = Nature | volume = 395 | issue = 6705 | pages = 917–21 | year = 1998 | pmid = 9804427 | doi = 10.1038/27699 | bibcode = 1998Natur.395..917T | s2cid = 4355885 }}</ref>
* [HDAC3](/source/HDAC3),<ref name = pmid11470869/>
* [MTA2](/source/MTA2),<ref name = pmid12920132/><ref name = pmid10444591/>
* [RB](/source/Retinoblastoma_protein),<ref name = pmid11470869/><ref name = pmid7503932>{{cite journal |author2-link=Eva Y.-H. P. Lee |vauthors=Qian YW, Lee EY | title = Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast | journal = J. Biol. Chem. | volume = 270 | issue = 43 | pages = 25507–13 | year = 1995 | pmid = 7503932 | doi = 10.1074/jbc.270.43.25507| doi-access = free }}</ref><ref name = pmid10734134>{{cite journal |vauthors=Nicolas E, Morales V, Magnaghi-Jaulin L, Harel-Bellan A, Richard-Foy H, Trouche D | title = RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein | journal = J. Biol. Chem. | volume = 275 | issue = 13 | pages = 9797–804 | year = 2000 | pmid = 10734134 | doi = 10.1074/jbc.275.13.9797| doi-access = free }}</ref>
* [SAP30](/source/SAP30),<ref name = pmid10444591/><ref name = pmid9651585/><ref name = pmid11784859>{{cite journal |vauthors=Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D | title = Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1) | journal = Mol. Cell. Biol. | volume = 22 | issue = 3 | pages = 835–48 | year = 2002 | pmid = 11784859 | pmc = 133546 | doi = 10.1128/MCB.22.3.835-848.2002}}</ref>  and
* [SIN3A](/source/SIN3A).<ref name = pmid9150133/><ref name = pmid9651585>{{cite journal |vauthors=Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D | title = SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex | journal = Mol. Cell | volume = 1 | issue = 7 | pages = 1021–31 | year = 1998 | pmid = 9651585 | doi = 10.1016/S1097-2765(00)80102-1| doi-access = free }}</ref>
{{Clear}}

==References==
{{Reflist|35em}}

==Further reading==
{{Refbegin|35em}}
* {{Cite web|title=RBBP4 retinoblastoma binding protein 4 &#91;Homo sapiens (human)&#93; |url=https://www.ncbi.nlm.nih.gov/gene/5928|publisher=[National Center for Biotechnology Information (NCBI)](/source/National_Center_for_Biotechnology_Information)|access-date=2013-09-06|location=Bethesda, MD}}
* {{cite journal |author=Bauw G |title=Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes |journal=Electrophoresis |volume=11 |issue= 7 |pages= 528–36 |year= 1990 |pmid= 1699755 |doi= 10.1002/elps.1150110703 |author2=Rasmussen HH |author3=van den Bulcke M |last4=Damme |first4=Jozef Van |last5=Puype |first5=Magda |last6=Gesser |first6=Borbala |last7=Celis |first7=Julio E. |last8=Vandekerckhove |first8=Joël|s2cid=24768114 }}
* {{cite journal |vauthors=Grozinger CM, Hassig CA, Schreiber SL |title=Three proteins define a class of human histone deacetylases related to yeast Hda1p |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 9 |pages= 4868–73 |year= 1999 |pmid= 10220385 |doi=10.1073/pnas.96.9.4868 |pmc=21783|bibcode=1999PNAS...96.4868G |doi-access=free }}
* {{cite journal |author=Hassig CA |title=A role for histone deacetylase activity in HDAC1-mediated transcriptional repression |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 7 |pages= 3519–24 |year= 1998 |pmid= 9520398 |doi=10.1073/pnas.95.7.3519 |pmc=19868 |author2=Tong JK |author3=Fleischer TC |last4=Owa |first4=T |last5=Grable |first5=PG |last6=Ayer |first6=DE |last7=Schreiber |first7=SL|bibcode=1998PNAS...95.3519H |doi-access=free }}
* {{cite journal |author=Marheineke K |author2=Krude T |title=Nucleosome assembly activity and intracellular localization of human CAF-1 changes during the cell division cycle |journal=J. Biol. Chem. |volume=273 |issue= 24 |pages= 15279–86 |year= 1998 |pmid= 9614144 |doi=10.1074/jbc.273.24.15279|doi-access=free }}
* {{cite journal |author=Maruyama K |author2=Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8}}
* {{cite journal |author=Qian YW |author2=Lee EY |title=Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast |journal=J. Biol. Chem. |volume=270 |issue= 43 |pages= 25507–13 |year= 1995 |pmid= 7503932 |doi=10.1074/jbc.270.43.25507|doi-access=free }}
* {{cite journal |author=Rasmussen HH |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=10.1002/elps.11501301199 |author2=van Damme J |author3=Puype M |last4=Gesser |first4=Borbala |last5=Celis |first5=Julio E. |last6=Vandekerckhove |first6=Joël|s2cid=41855774 }}
* {{cite journal |author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |author2=Yoshitomo-Nakagawa K |author3=Maruyama K |last4=Suyama |first4=Akira |last5=Sugano |first5=Sumio}}
* {{cite journal |vauthors=Taunton J, Hassig CA, Schreiber SL |title=A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p |journal=Science |volume=272 |issue= 5260 |pages= 408–11 |year= 1996 |pmid= 8602529 |doi=10.1126/science.272.5260.408|bibcode=1996Sci...272..408T |s2cid=25717734 }}
* {{cite journal |author=Tong JK |title=Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex |journal=Nature |volume=395 |issue= 6705 |pages= 917–21 |year= 1998 |pmid= 9804427 |doi= 10.1038/27699 |author2=Hassig CA |author3=Schnitzler GR |last4=Schnitzler |first4=Gavin R. |last5=Kingston |first5=Robert E.|bibcode=1998Natur.395..917T |s2cid=4355885 }}
* {{cite journal |author=Verreault A |author2=Kaufman PD |author3=Kobayashi R, Stillman B |title=Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase |journal=Curr. Biol. |volume=8 |issue= 2 |pages= 96–108 |year= 1998 |pmid= 9427644 |doi=10.1016/S0960-9822(98)70040-5|s2cid=201273 |doi-access=free |bibcode=1998CBio....8...96V }}
* {{cite journal |author=Verreault A |author2=Kaufman PD |author3=Kobayashi R, Stillman B |title=Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4 |journal=Cell |volume=87 |issue= 1 |pages= 95–104 |year= 1996 |pmid= 8858152 |doi=10.1016/S0092-8674(00)81326-4|s2cid=1416453 |doi-access=free }}
* {{cite journal |author=Wolffe AP |author2=Urnov FD |author3=Guschin D |title=Co-repressor complexes and remodelling chromatin for repression |journal=Biochem. Soc. Trans. |volume=28 |issue= 4 |pages= 379–86 |year= 2001 |pmid= 10961924 |doi=10.1042/0300-5127:0280379}}
* {{cite journal |author=Yarden RI |author2=Brody LC |title=BRCA1 interacts with components of the histone deacetylase complex |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 9 |pages= 4983–8 |year= 1999 |pmid= 10220405 |doi=10.1073/pnas.96.9.4983 |pmc=21803|bibcode=1999PNAS...96.4983Y |doi-access=free }}
* {{cite journal |author=Zhang Y |title=Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation |journal=Genes Dev. |volume=13 |issue= 15 |pages= 1924–35 |year= 1999 |pmid= 10444591 |doi=10.1101/gad.13.15.1924 |pmc=316920 |author2=Ng HH |author3=Erdjument-Bromage H |last4=Tempst |first4=P. |last5=Bird |first5=A. |last6=Reinberg |first6=D.}}
* {{cite journal |author=Zhang Y |title=Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex |journal=Cell |volume=89 |issue= 3 |pages= 357–64 |year= 1997 |pmid= 9150135 |doi=10.1016/S0092-8674(00)80216-0 |author2=Iratni R |author3=Erdjument-Bromage H |last4=Tempst |first4=Paul |last5=Reinberg |first5=Danny|doi-access=free }}
* {{cite journal |author=Zhang Y |title=SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex |journal=Mol. Cell |volume=1 |issue= 7 |pages= 1021–31 |year= 1998 |pmid= 9651585 |doi=10.1016/S1097-2765(00)80102-1 |author2=Sun ZW |author3=Iratni R |last4=Erdjument-Bromage |first4=Hediye |last5=Tempst |first5=Paul |last6=Hampsey |first6=Michael |last7=Reinberg |first7=Danny|doi-access=free }}
* {{cite journal |author=Zhang Y |title=The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities |journal=Cell |volume=95 |issue= 2 |pages= 279–89 |year= 1998 |pmid= 9790534 |doi=10.1016/S0092-8674(00)81758-4 |author2=LeRoy G |author3=Seelig HP |last4=Lane |first4=William S |last5=Reinberg |first5=Danny|s2cid=18786866 |doi-access=free }}
* {{cite journal |author=Zhang Y |author2=Dufau ML |title=Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes |journal=J. Steroid Biochem. Mol. Biol. |volume=85 |issue= 2–5 |pages= 401–14 |year= 2003 |pmid= 12943729 |doi=10.1016/S0960-0760(03)00230-9|s2cid=28512341 |url=https://zenodo.org/record/1260176}}

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Adapted from the Wikipedia article [RBBP4](https://en.wikipedia.org/wiki/RBBP4) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/RBBP4?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.