Ask about this productRelated genes to: RNF31 Blocking Peptide
- Gene:
- RNF31 NIH gene
- Name:
- ring finger protein 31
- Previous symbol:
- -
- Synonyms:
- ZIBRA, FLJ10111, FLJ23501, HOIP, Paul
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-29
- Date modifiied:
- 2019-04-23
Related products to: RNF31 Blocking Peptide
Related articles to: RNF31 Blocking Peptide
- PANoptosis is a newly discovered form of programmed cell death. Accumulating studies confirmed that long non-coding RNAs (lncRNAs) play crucial role in colorectal cancer (CRC) progression. However, the role of PANoptosis-related lncRNAs in CRC has not yet been elucidated. In the current study, we used a bioinformatics pipeline to find important lncRNAs in CRC. Based on the results of in silico step, we selected RNF31, and three related lncRNAs, namely SNHG12, ASMTL-AS1 and LMNTD2-AS1 to assess their expression in 45 paired CRC and adjacent non-tumor samples. Compared with matched ANT samples, ASMTL-AS1 and SNHG12 were markedly upregulated in tumor tissues (mean fold-change 7.53, 95% CI 1.64-34.53, P = 0.009; and 8.66, 95% CI 3.15-23.78, P < 0.0001, respectively), whereas LMNTD2-AS1 was strongly downregulated (mean fold-change 0.06, 95% CI 0.014-0.26, P = 0.0004), corresponding to an approximately 16-fold reduction in tumor tissues. RNF31 showed a non-significant increase (mean fold-change 2.77, 95% CI 0.77-9.97, P = 0.15). Multivariate logistic regression incorporating all four transcripts (RNF31, ASMTL-AS1, LMNTD2-AS1, and SNHG12) demonstrated promising diagnostic performance with an AUC of 0.88 (95% CI: 0.80-0.95, P < 0.0001). These results inspire further experiments to clarify underlying mechanisms and translational studies to assess potential of mentioned lncRNAs as biomarkers. - Source: PubMed
Publication date: 2026/09/21
Sanati MahlaEslami SolatFazeli ZahraGhadyani FatemehGhafouri-Fard SoudehSadeghi Amir - The mechanisms governing PD-L1 expression in breast cancer are highly complex and context-dependent. This article proposes a novel "dual-track" regulatory model to resolve the conflicting roles of estrogen in tumor immunity. Genomic signaling through ER-α suppresses PD-L1 transcription, explaining lower PD-L1 levels in ER-α-positive tumors. Conversely, non-genomic signaling mediated by cell-surface integrin αvβ3 drives PD-L1 presentation by triggering downstream PI3K/Akt and MAPK/ERK 1/2 pathways. We synthesize emerging data on how post-translational modulators (RNF31, p66Shc) and metabolic regulators (SIRT1-NAD+ axis) fine-tune PD-L1 stability. This interplay reveals a therapeutic vulnerability: antiestrogen treatments can paradoxically increase surface PD-L1 expression. In triple-negative breast cancer (TNBC), the absence of ER-α combined with active integrin αvβ3 signaling accelerates PD-L1-mediated immune evasion. This comprehensive framework uncovers novel molecular targets to improve combined endocrine and immunotherapeutic regimens for breast cancer patients. - Source: PubMed
Publication date: 2026/08/04
Crawford Dana RYang Yung-NingLiu Feng-ChengLin Chun-MaoYang Yu-Chen S HLi Zi-LinShih Ya-JungMo Ju-KuYao Chih-JungLin Hung-YunWang Kuan - Yes-associated protein (YAP), a key effector of the Hippo pathway, plays a well-established role in colorectal cancer (CRC). However, the functional relevance of site-specific post-translational modifications (PTMs) in YAP, particularly methylation, remains insufficiently explored. SET-domain-containing protein 8 (SETD8), the sole mono-methyltransferase for histone 4 lysine 20 (H4K20), is implicated in various cancers, yet its biological function and underlying mechanisms in CRC are elusive. While SETD8 is primarily known for its histone methylation activity, its capacity to modify non-histone proteins, such as YAP, remains largely unexplored. This study aimed to demonstrate that SETD8 exerted a tumor-suppressive effect on CRC by inhibiting YAP protein expression. Mechanistically, SETD8 physically interacts with YAP to catalyze mono-methylation at lysine 76 (K76me). This modification enhances the interaction between YAP and the E3 ubiquitin ligase RING finger protein 31 (RNF31), promoting YAP K48-linked polyubiquitination and subsequent proteasomal degradation. Clinically, patients with CRC and high SETD8 expression, including elevated YAP K76me levels, exhibited favorable pathological grading and improved prognosis. Collectively, our findings identify a novel SETD8-YAP K76me regulatory axis that restricts CRC progression, suggesting that targeting this axis may represent a promising therapeutic strategy. - Source: PubMed
Publication date: 2026/07/29
Yu YaliWang HailinWu JiangNie HaihangHong YuntianZhou JingkaiLu JialiYuan YuanZhang YukangLi LianyunWu MinZhao QiuXu FeiYe Mei - Targeting macrophage polarization to restore immunological balance is a promising treatment strategy for ulcerative colitis (UC). This study aims to explore the preventive effects of benzoylpaeoniflorin (BPF) for UC and to elucidate the underlying mechanisms. - Source: PubMed
Publication date: 2026/07/26
Yang ZhouyuLi KeLi XinruZhong PeiHu YuqianYao Xin - Molecular recognition is governed not only by the structural complementarity of the final complex, but by the kinetic pathway through which it forms. Polyubiquitin chains, in which sequence-identical domains are covalently linked yet must be discriminated by dedicated receptors to encode distinct cellular signals, exemplify this challenge. For NMR relaxation dispersion studies of such systems, spectral overlap between identical domains prevents conventional uniform isotope labeling from resolving the per-domain exchange contributions. Here we show, using domain-selective 15N labeling combined with R2 relaxation dispersion, that the binding of linear (Met1-linked) diubiquitin to HOIL-1L NZF proceeds through an apparent three-state pathway as detected by relaxation dispersion, in which rapid ligand-dependent pre-equilibration populates a conformationally preorganized intermediate that is selectively captured by NZF in a slower, chain-type-selective step. This kinetic hierarchy offers a mechanistic basis for understanding the discrimination between linear and Lys63-linked ubiquitin chains that static structures alone cannot reveal. This strategy should be broadly applicable to multidomain recognition systems─including epigenetic reader complexes and multivalent signaling adaptors─where the pathway between known structural end points remains hidden. - Source: PubMed
Walinda ErikIshii NaokiMorimoto DaichiSugase Kenji