Disease relevance of RBBP4

• RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein [1].
• Our results show that RbAp48 is a NF-kappaB-regulated gene playing an important role in thyroid cancer cell autonomous proliferation [2].

High impact information on RBBP4

• RNAi knockdown in human cells shows that Mis16 function is conserved as RbAp48 and RbAp46 are both required for localization of human CENP-A [3].
• In mammals, Rb and related proteins act as regulators of E2F transcription factors, and RbAp48 may act with such proteins as a transcriptional corepressor [4].
• The human SAP30 complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones due to the inability of the histone binding proteins RbAp46 and RbAp48 to gain access to nucleosomal histones [5].
• Two closely related mammalian RB binding proteins, RbAp48 and RbAp46, share sequence homology with the Msi1 protein of yeast [6].
• Human RbAp48 is present in protein complexes involved in histone acetylation and chromatin assembly [6].

Biological context of RBBP4

• Reducing the expression of RbAp48 through small interfering RNA inhibits the apoptosis [7].
• One of the strongest interactions identified the histone binding protein RbAp48 [8].
• These data indicate that the association of phosphorylated CREB with CBP promotes the binding of RbAp48 and its homologue RbAp46, allowing the formation of a complex that facilitates histone acetylation during transcriptional activation [8].
• Interestingly, the mouse and human RbAp48 amino acid sequences are completely identical, and the mouse and human RbAp46 differ only by one conserved amino acid substitution [9].
• These results suggest that RbAp48 and RbAp46 may have shared as well as unique functions in the regulation of cell proliferation and differentiation [9].

Anatomical context of RBBP4

• Indeed, transgenic expression of the RbAp48 gene induced apoptosis in the exocrine glands but not in other organs [7].
• Exogenous RPD3 may be targeted to histones through interaction with endogenous RbAp48 to direct transcriptional repression of the Xenopus TRbetaA promoter in the oocyte nucleus [10].
• To biologically validate our classifier, we transfected RbAp48 into three cancer cell lines (HS-578T, MALME-3M, and MDA-MB-231) [11].
• To examine the Jurkat cell interaction partners of RbAp48, we digested entire immunoaffinity extracts with trypsin and identified potential interacting proteins using one- and two-dimensional microcapillary HPLC-ion-trap mass spectrometry [12].

Associations of RBBP4 with chemical compounds

• Novel role for RbAp48 in tissue-specific, estrogen deficiency-dependent apoptosis in the exocrine glands [7].

Other interactions of RBBP4

• A subset of these mutations also cause a decreased interaction with the HDAC1-associated proteins RbAp48 and mSin3A [13].
• A multiprotein complex is recruited to the hLHR promoter via interaction with Sp1/Sp3: HDACs dock directly to Sp1-1 bound DNA and indirectly to Sp3-1 bound DNA through RbAp48, while mSin3A interacts HDACs and potentiates HDAC1-mediated repression [14].
• Here we report that BRCA1 interacts in vivo and in vitro with the Rb-binding proteins, RbAp46 and RbAp48, as well as with Rb [15].
• CTIP2 was found to associate with the NuRD complex through direct interaction with both RbAp46 and RbAp48, and components of the NuRD complex were found to be recruited to an artificial promoter template in a CTIP2-dependent manner in transfected cells [16].
• The genes encoding Beclin 1, RbAp48, Pir51 and aldolase b are first reported that may be related with hepatocarcinoma [17].

Analytical, diagnostic and therapeutic context of RBBP4

• There was little overlap with RbAp48-interacting proteins defined by yeast two-hybrid methods [12].

References