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RBBP6 might potentiate cervical carcinoma cell viability.
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Results from a study on gene expression variability markers in early-stage human embryos shows that RBBP6 is a putative expression variability marker for the 3-day, 8-cell embryo stage.
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RBBP6 overexpression could resist colorectal cancer cells against radiation.
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These results suggest that the RBBP6-3 isoform may be involved in promoting apoptosis in cancerous cells.
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RBBP6 is a candidate gene for myeloproliferative neoplasms (MPNs) susceptibility in a subset of pedigrees with familial MPN.
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High expression levels of RBBP6 and high apoptosis levels were found in HIV-associated nephropathy (HIVAN) cases. This direct association between RBBP6 expression and apoptosis levels suggests that RBBP6 play a role in HIVAN pathogenesis.
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gene silencing sensitises breast cancer cells to staurosporine and camptothecin-induced cell death
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RBBP6 prevents DNA damage by destabilizing the transcriptional repressor ZBTB38.
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RBBP6 gene variants are associated with glioma and contribute to glioma susceptibility
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implicate RBBP6 and iso3 as novel regulators of 3' processing, especially of RNAs with AU-rich 3' UTRs.
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these findings suggest that RBBP6 isoform 3 is a cell cycle regulator and may be deregulated in carcinogenesis
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AGO2, PACT and TRBP are required for the efficient functioning of Dicer in cells
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Taken together with the structural similarities to U-box-containing proteins, our data suggest that RBBP6 plays a role in chaperone-mediated ubiquitination and possibly in protein quality control.
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RBBP6 may be involved in the degradation of p53, thereby enhancing cell proliferation and inhibiting apoptosis in lung cancer.
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P2P-R expression may be translationally regulated by PUM2 and that P2P-R may modulate translation by influencing ribosomal protein gene expression
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RBBP6 has a role in mRNA processing and ubiquitin-like pathways
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The authors showed that RBBP6 and its isolated RING finger domain were able to ubiquitinate YB-1, resulting in its degradation in the proteosome. As a result, RBBP6 was able to suppress the levels of YB-1 in vivo and reduce its transactivational ability.
