RYBP (RING1 And YY1 Binding Protein)

In summary, the present study demonstrated that RP11-196G11.6 may inhibit NB progression by sponging miR-376a-3p, leading to the upregulation of RYBP expression and consequently inhibiting NB progression. These findings revealed a novel lncRNA-miRNA axis involved in NB pathogenesis.

RYBP cooperates with TrxG component to regulate SE activity. Dysfunction of RYBP relates to various diseases. The findings provide new insights into the transcriptionally active function of Polycomb protein in cell fate determination.

Compared to low glucose culture and their wildtypes, high glucose significantly enhanced tumor cell migration in RYBP knockdown or knockout tumor cells. Taken together, our current study uncovered a previously unknown function of RYBP in tumor metabolism, and this finding will enhance the exploration of the interplay between RYBP and nutrients during tumor cell metabolic reprogramming.

In addition, endogenous RYBP overexpression enhanced sensitivity to oxaliplatin. Therefore, RYBP may contribute to improved prognosis in CRC by regulating the cell cycle, apoptosis and oxaliplatin sensitivity via the p53‑mediated pathway.

We also show that overexpression of RYBP hinders cancer cell migration through, at least in part, ATM inhibition. We provide new mechanism(s) by which RYBP expression may sensitize cancer cells to DNA damaging agents and inhibits cancer metastasis.

BCL-2 specific inhibitor ABT-199 significantly induces cell apoptosis in RYBP-depleted cells, and restores the apoptosis sensitivity to etoposide and decitabine. RYBP inhibition leads to epigenetic overexpression of anti-apoptotic protein BCL2 in MDS, which contributes to apoptotic resistance of clonal cells and disease progression. BCL2 inhibitor may be considered as a candidate agent in advanced MDS.