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
- 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 - A persistent evolutionary arms race exists between enteroviruses and their hosts, in which viruses employ multiple strategies to antagonize host antiviral defenses and sustain efficient replication. However, how host restriction factors are broadly targeted by enteroviruses during this process, as well as the underlying molecular mechanisms, remain poorly understood. Here, we identify ring finger protein 31 (RNF31) as a previously unrecognized host restriction factor that limits enterovirus A71 (EV-A71) replication through a dual antiviral mechanism. Specifically, RNF31 enhances innate antiviral immune signaling by promoting K63-linked polyubiquitination of Retinoic acid-inducible gene I (RIG-I). Simultaneously, RNF31 directly suppresses EV-A71 replication by inducing K27- and K48-linked polyubiquitination of the Viral Protein 4 (VP4), thereby resulting in its proteasome-dependent degradation. Furthermore, we demonstrate that the viral 3C protease (3Cpro) cleaves RNF31 at residue Q400, abolishing both RNF31-mediated activation of innate immunity and VP4 degradation, ultimately resulting in the loss of its antiviral activity. Notably, 3Cpro from multiple enteroviruses, including Coxsackievirus A16 (CV-A16), Coxsackievirus B3 (CV-B3), and Enterovirus D68 (EV-D68), cleave RNF31 at this same conserved site. Consistent with these findings, RNF31 significantly inhibits the replication of these diverse enteroviruses. Collectively, this study establishes RNF31 as a host restriction factor that suppresses the replication of multiple enteroviruses and reveals a shared immune evasion strategy employed by enteroviruses. - Source: PubMed
Publication date: 2026/07/02
Zhang QingxiangGao YuanGao WenyingZhang XueXu ShengyuanZhang Wenyan