RBM14

Last update 08 May 2025

Basic Info

Synonyms

COAA, DKFZp779J0927, Paraspeckle protein 2

+ [10]

Introduction

Isoform 1 may function as a nuclear receptor coactivator, enhancing transcription through other coactivators such as NCOA6 and CITED1. Isoform 2, functions as a transcriptional repressor, modulating transcriptional activities of coactivators including isoform 1, NCOA6 and CITED1 (PubMed:11443112). Regulates centriole biogenesis by suppressing the formation of aberrant centriolar protein complexes in the cytoplasm and thus preserving mitotic spindle integrity. Prevents the formation of the STIL-CPAP complex (which can induce the formation of aberrant centriolar protein complexes) by interfering with the interaction of STIL with CPAP (PubMed:25385835). Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Also involved in the regulation of pre-mRNA alternative splicing (PubMed:37548402).

100 Clinical Results associated with RBM14

100 Translational Medicine associated with RBM14

0 Patents (Medical) associated with RBM14

131

Literatures (Medical) associated with RBM14

17 Apr 2025·Combinatorial Chemistry & High Throughput Screening

Identification of the Role of Necroptosis-Related Genes in the Oxidative Damage of Lens Epithelial Cells and Validation in Ultraviolet B-induced Cataract in Rats

Article

Author: Zhong, Xin ; Liang, Hao ; Lan, Tian ; Yang, Yingqin ; Gan, Qingqiao ; Liang, Yongshun

Introduction:The specific role of necroptosis in the pathogenesis of cataracts remains unclear. This study aimed to identify and validate the genes related to necroptosis in the development of cataracts through bioinformatics analysis.Method:We utilized RNA sequencing data (GSE161701) from the Gene Expression Omnibus (GEO) database and employed R software to perform differential expression analysis of necroptosis- related genes (NRGs) in lens epithelial cells (LECs) under oxidative stress. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses were conducted to evaluate the functions of necroptosis-related differentially expressed genes (NRDEGs) and their associated pathways. Additionally, a diagnostic model was established using LASSO regression to select hub genes, and protein-protein interaction (PPI) networks, mRNA-miRNA, and mRNAdrug regulatory networks were constructed. Immune infiltration analysis was performed using the xCell and CIBERSORT algorithms, and the differential expression of hub genes was validated in a UVB-induced rat cataract model using RT-qPCR and immunohistochemistry.Results:The results indicated that oxidative stress promoted necroptosis in LECs, involving 86 NRDEGs and nine hub genes. GO and KEGG analyses revealed significant enrichment in necroptosis- associated pathways. Furthermore, we identified 58 mRNA-miRNA interactions and 131 potential molecular compounds or drugs. The immune infiltration analysis showed that certain immune cells exhibited significantly elevated expression in the cataract group, with notable correlations between some immune cells and hub genes. RT-qPCR and immunohistochemistry confirmed the expression of 9 hub genes and 3 key necroptosis genes. BAX, CXCL1, EPAS1, JUN, LRP1, RBM14, SERTAD1, and TNFAIP3 were highlighted as potential diagnostic and therapeutic targets.Conclusion:This study identified key NRDEGs involved in the pathogenesis of cataracts under oxidative stress through bioinformatics analyses, potentially providing new targets and research directions for future cataract prevention and treatment.

01 Apr 2025·International Journal of Biological Macromolecules

Subcellular proteomics reveals the crosstalk between nucleocytoplasmic trafficking and the innate immune response to Senecavirus A infection

Article

Author: Zhang, Gaiping ; Wan, Haocheng ; Zhang, Linru ; Deng, Xiaoshuang ; Shi, Yan ; Zhang, Yuhang ; Zhou, Menghan ; Wan, Bo ; Jiang, Dawei ; Du, Yongkun ; Hu, Man ; Li, Mingyang ; He, Wenrui ; Han, Shichong

Mounting evidence suggests that a number of host nuclear-resident proteins are indispensable for the replication of picornaviruses, a typical class of cytoplasmic RNA viruses. Host nucleocytoplasmic transport is often hijacked by viruses to promote their replication in the cytoplasm of infected cells, and suppress the innate immune response. However, little is known about the mechanisms by which Senecavirus A (SVA) manipulates nucleocytoplasmic trafficking events to promote infection. In this study, we combined subcellular fractionation with quantitative protein mass spectrometry to systematically explore the dynamics of host cell nuclear protein relocalization to the cytoplasm during SVA infection. Our analysis revealed 484 differentially relocalized proteins with important roles in a variety of fundamental cellular processes, including a marked enrichment in nucleocytoplasmic transport proteins, confirming viral subversion of this pathway. Further analysis uncovered a highly selective translocation of nuclear proteins involved in the antiviral innate immune response, including SIN3 Transcription Regulator Family Member A (SIN3A) and RNA Binding Motif Protein 14 (RBM14). Using a series of sophisticated molecular cell manipulation techniques and viral replication assays, we further demonstrated that SIN3A suppresses the innate antiviral immune response and facilitates SVA replication, whereas RBM14 promotes innate immunity and inhibits viral replication. This indicates that nucleocytoplasmic shuttling of these nuclear proteins is critical for the regulation of the host innate immune response to SVA infection. This is the first study to reveal dramatic changes in nuclear/cytoplasmic compartmentalization of host proteins during SVA infection and characterize their key roles in antiviral innate immunity.

10 Jan 2025·Science Advances

Infection-induced lysine lactylation enables herpesvirus immune evasion

Article

Author: Tyl, Matthew D. ; Merengwa, Victoria U. ; Cristea, Ileana M.

Aerobic glycolysis is a hallmark of many viral infections, leading to substantial accumulation of lactate. However, the regulatory roles of lactate during viral infections remain poorly understood. Here, we report that human cytomegalovirus (HCMV) infection leverages lactate to induce widespread protein lactylation and promote viral spread. We establish that lactyllysine is enriched in intrinsically disordered regions, regulating viral protein condensates and immune signaling transduction. Dynamic lactylation of immune factors suppresses immunity, a feature we show to be shared for HCMV and herpes simplex virus 1 infections, through regulation of RNA binding protein 14 and interferon-γ–inducible protein 16 (IFI16). K90 lactylation of the viral DNA sensor IFI16 inhibits recruitment of the DNA damage response kinase DNA-PK, preventing IFI16-driven virus gene repression and cytokine induction. Together, we characterize global protein lactylation dynamics during virus infection, finding that virus-induced lactate contributes to its immune evasion through direct inhibition of immune signaling pathways.

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