| Long noncoding RNA AC245100.4 promotes prostate cancer tumorigenesis via the microRNA1455p/RBBP5 axis. | Long non‑coding RNA AC245100.4 promotes prostate cancer tumorigenesis via the microRNA‑145‑5p/RBBP5 axis.
Xie H, Zhao J, Wan J, Zhao J, Wang Q, Yang X, Yang W, Lin P, Yu X., Free PMC Article | 11/22/2021 |
| We used a hybrid methods approach to study the assembly and biochemical function of the minimally active MLL1 complex (MLL1, WDR5 and RbBP5)..We identified a new interaction site between the MLL1 SET domain and the WD40 beta-propeller domain of RbBP5, and demonstrate the susceptibility of the catalytic function of the complex to disruption of individual interaction sites. | The MLL1 trimeric catalytic complex is a dynamic conformational ensemble stabilized by multiple weak interactions.
Kaustov L, Lemak A, Wu H, Faini M, Fan L, Fang X, Zeng H, Duan S, Allali-Hassani A, Li F, Wei Y, Vedadi M, Aebersold R, Wang Y, Houliston S, Arrowsmith CH., Free PMC Article | 12/14/2019 |
| We identified an internal interaction between the WD40 propeller and the C-terminal distal region in RBBP5, which assisted the maintenance of the compact conformation of the MLL1 complex. We also discovered a vertebrate-specific motif in the C-terminal distal region of RBBP5 that contributed to nucleosome recognition and methylation of nucleosomes by the MLL1 complex. | The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex.
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y., Free PMC Article | 12/14/2019 |
| Our nuclear magnetic resonance binding data supports the hypothesis that in addition to the role of RbBP5 in catalytic activation, its beta-propeller domain is a platform for the recruitment of the MLL complexes to chromatin targets through its direct interaction with nucleic acids. | The structure of the RbBP5 β-propeller domain reveals a surface with potential nucleic acid binding sites.
Mittal A, Hobor F, Zhang Y, Martin SR, Gamblin SJ, Ramos A, Wilson JR., Free PMC Article | 07/20/2019 |
| RBBP5 plays an important role in the progression of hepatocellular carcinoma. | Retinoblastoma Binding Protein 5 Correlates with the Progression in Hepatocellular Carcinoma.
Zhou H, Bao J, Zhu X, Dai G, Jiang X, Jiao X, Sheng H, Huang J, Yu H., Free PMC Article | 03/23/2019 |
| Results from a study on gene expression variability markers in early-stage human embryos shows that RBBP5 is a putative expression variability marker for the 3-day, 8-cell embryo stage. | Variability of Gene Expression Identifies Transcriptional Regulators of Early Human Embryonic Development.
Hasegawa Y, Taylor D, Ovchinnikov DA, Wolvetang EJ, de Torrenté L, Mar JC., Free PMC Article | 07/23/2018 |
| this study shows that during epithelial-mesenchymal transition in the prostate cancer cell line RbBP5 binding is increased in the vicinity of Snail transcription start site | Role of RbBP5 and H3K4me3 in the vicinity of Snail transcription start site during epithelial-mesenchymal transition in prostate cancer cell.
Li D, Sun H, Sun WJ, Bao HB, Si SH, Fan JL, Lin P, Cui RJ, Pan YJ, Wen SM, Zheng XL, Yu XG., Free PMC Article | 02/24/2018 |
| different cancer mutations in MLL1 lead to a loss or increase in activity, illustrating the complex and tumor-specific role of MLL1 in carcinogenesis. | Somatic cancer mutations in the MLL1 histone methyltransferase modulate its enzymatic activity and dependence on the WDR5/RBBP5/ASH2L complex.
Weirich S, Kudithipudi S, Jeltsch A., Free PMC Article | 11/4/2017 |
| role of RBQ3 in the development of multiple myeloma | RBQ3 participates in multiple myeloma cell proliferation, adhesion and chemoresistance.
Liu H, Ding L, Shen Y, Zhong F, Wang Q, Xu X. | 03/11/2017 |
| This study demonstrated that RBQ3 might play an important role in glioma, and RBQ3 inhibitors might be novel anti-tumor agents. | Expression and clinical role of RBQ3 in gliomas.
Zhao C, Chen W, Dai S, Zhang X, Ban N, Fan S, Bao Z, Sun J, Shen C, Xia X, Zhang L, Ren J. | 10/1/2016 |
| The identified components revealed factors involved in histone methylation and cell cycle control and include Ash2L, RbBP5, WDR5, HCF-1, DBC-1, and EMSY. | Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation.
Garapaty S, Xu CF, Trojer P, Mahajan MA, Neubert TA, Samuels HH., Free PMC Article | 07/12/2016 |
| Non active site mutations in the MLL1 SET domain render the protein defective for H3K4 dimethylation by the MLL1 core complex, which is associated with a loss of the ability of MLL1 to interact with WRAD or with the RbBP5/Ash2L heterodimer. | A non-active-site SET domain surface crucial for the interaction of MLL1 and the RbBP5/Ash2L heterodimer within MLL family core complexes.
Shinsky SA, Hu M, Vought VE, Ng SB, Bamshad MJ, Shendure J, Cosgrove MS., Free PMC Article | 07/12/2014 |
| Data indicate that MLL1 methylates Ash2L in the absence of histone H3, but only when assembled within a complex with WDR5 and RbBP5. | Automethylation activities within the mixed lineage leukemia-1 (MLL1) core complex reveal evidence supporting a "two-active site" model for multiple histone H3 lysine 4 methylation.
Patel A, Vought VE, Swatkoski S, Viggiano S, Howard B, Dharmarajan V, Monteith KE, Kupakuwana G, Namitz KE, Shinsky SA, Cotter RJ, Cosgrove MS., Free PMC Article | 04/12/2014 |
| structural and biochemical analyses reveal a basic surface on Ash2L as the RbBP5-binding interface, and this interface is crucial for both RbBP5 binding and MLL1 methyltransferase activity regulation | Structure of the SPRY domain of human Ash2L and its interactions with RbBP5 and DPY30.
Chen Y, Cao F, Wan B, Dou Y, Lei M., Free PMC Article | 07/14/2012 |
| MLL1 SET domain make direct contacts with the substrates and contribute to the formation of a joint catalytic center. | An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain.
Cao F, Chen Y, Cierpicki T, Liu Y, Basrur V, Lei M, Dou Y., Free PMC Article | 04/30/2011 |
| Results show that Depletion of CHD8 enhances HOXA2 expression and a loss of the WDR5/Ash2L/RbBP5 subcomplex. | Regulation of HOXA2 gene expression by the ATP-dependent chromatin remodeling enzyme CHD8.
Yates JA, Menon T, Thompson BA, Bochar DA. | 05/10/2010 |
| analysis of menin's role as a tumor suppressor and binding sites of Rbbp5 and MLL1 | Genome-wide analysis of menin binding provides insights into MEN1 tumorigenesis.
Scacheri PC, Davis S, Odom DT, Crawford GE, Perkins S, Halawi MJ, Agarwal SK, Marx SJ, Spiegel AM, Meltzer PS, Collins FS., Free PMC Article | 01/21/2010 |