RYBP modulates stability and function of Ring1B through targeting UBE3A
Explore this paper's citation graph
Summary
It is shown that RYBP inhibits the polyubiquitination‐mediated proteasomal degradation of RingIB independently of its ubiquitin (Ub)‐protein isopeptide ligase (E3) ligase activity, leading to its stabilization and increased catalytic activity toward monoubiquitinated degradation of histone H2A at lysine 119.
- Type
- article
- Published
- 2018-07-24
- Cited by
- 4
- References
- 54
- OpenAlex
- https://openalex.org/W2883094845
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:51716120
Keywords
Ubiquitin ligase, UBE3A, Ubiquitin, Cell biology, Repressor
References
- RYBP expression is associated with better survival of patients with hepatocellular carcinoma (HCC) and responsiveness to chemotherapy of HCC cells in vitro and in vivo
- Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex
- The Polycomb group protein RING1B is overexpressed in ductal breast carcinoma and is required to sustain FAK steady state levels in breast cancer epithelial cells
- RYBP predicts survival of patients with non-small cell lung cancer and regulates tumor cell growth and the response to chemotherapy
- Roles of the Polycomb group proteins in stem cells and cancer
- Ring1B Compacts Chromatin Structure and Represses Gene Expression Independent of Histone Ubiquitination
- Adenoviral-mediated Rybp expression promotes tumor cell-specific apoptosis
- TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein
- Ring1B promotes hepatic stem/progenitor cell expansion through simultaneous suppression of Cdkn1a and Cdkn2a in mice
- A phosphorylated form of Mel-18 targets the Ring1B histone H2A ubiquitin ligase to chromatin.
- YEAF1/RYBP and YAF-2 Are Functionally Distinct Members of a Cofactor Family for the YY1 and E4TF1/hGABP Transcription Factors*
- Histone H2A Mono-Ubiquitination Is a Crucial Step to Mediate PRC1-Dependent Repression of Developmental Genes to Maintain ES Cell Identity
- The Polycomb‐associated protein Rybp is a ubiquitin binding protein
- Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function
- RNF2/Ring1b negatively regulates p53 expression in selective cancer cell types to promote tumor development
- Regulation of the Polycomb protein RING1B ubiquitination by USP7.
- RNF2 is recruited by WASH to ubiquitinate AMBRA1 leading to downregulation of autophagy
- PCGF Homologs, CBX Proteins, and RYBP Define Functionally Distinct PRC1 Family Complexes
- E6AP promotes the degradation of the PML tumor suppressor
- Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation.
Cited by
- Evolving Role of RING1 and YY1 Binding Protein in the Regulation of Germ-Cell-Specific Transcription
- RYBP inhibits esophageal squamous cell carcinoma proliferation through downregulating CDC6 and CDC45 in G1-S phase transition process.
- Polycomb group proteins in cancer: multifaceted functions and strategies for modulation
- Glucose-induced RYBP suppresses tumor cell aerobic glycolysis and migration.
Related papers
- Ube3a, the E3 ubiquitin ligase causing Angelman syndrome and linked to autism, regulates protein homeostasis through the proteasomal shuttle Rpn10
- Promiscuous Interactions of gp78 E3 ligase CUE domain with polyubiquitin chains
- Ubiquitination and Degradation of Mutant p53
- The Ubiquitin E3 Ligase MaLUL2 Is Involved in High Temperature-Induced Green Ripening in Banana Fruit
- Reconstitution and Structural Analysis of a HECT Ligase-Ubiquitin Complex via an Activity-Based Probe
- Down-Regulating Destruction: Phosphorylation Regulates the E3 Ubiquitin Ligase Nedd4-2
- Relationship between Ubiquitin Ligase and Connective Tissue Diseases
- Ubiquitin system: selectivity and timing of protein destruction.
- Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A