HNRNPA3

Last update 08 May 2025

Basic Info

Synonyms

heterogeneous nuclear ribonucleoprotein A3, hnRNP A3, HNRNPA3

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Introduction

Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing.

100 Clinical Results associated with HNRNPA3

100 Translational Medicine associated with HNRNPA3

0 Patents (Medical) associated with HNRNPA3

Literatures (Medical) associated with HNRNPA3

01 May 2025·Biochemical and Biophysical Research Communications

Putrescine modulates alternative splicing of gonadotropin hormone-releasing hormone (GnRH) through differential regulation of splicing factors

Article

Author: Gautam, Pooja ; Banerjee, Arnab ; Ghosh, Sayan ; Srivastava, Vijigisha ; Bammidi, Sridhar ; Babu, Vishnu Suresh

Gonadotropin-releasing hormone (GnRH) plays a critical role in reproductive function, with its activity influenced by differential splicing that generates functionally distinct isoforms. However, the molecular mechanisms regulating GnRH pre-mRNA processing remain poorly understood. In this study, we investigated the effects of putrescine, a biogenic polyamine, on GnRH splicing and the expression of splicing regulatory factors. Transcriptome analysis revealed that putrescine treatment induces significant changes in the expression of splicing-related genes. Notably, putrescine enhanced the expression of both the full-length GnRH isoform (GnRH V1) and an exon-skipped variant (GnRH V2), with the latter exhibiting higher expression levels. Further analysis showed putrescine significantly upregulated key alternative splicing regulators, including SR proteins (SRSF11, SRSF12), RNA helicases (DDX26B, DDX6, DDX25), and Pre-mRNA processing factor (PRPF8), Splicing factor 3b (SF3B2). Conversely, HnRNPA3 and SF3B1 were downregulated. These findings suggest putrescine influences GnRH isoform expression through a dual mechanism: enhancing factors that promote alternative splicing while simultaneously attenuating components of the canonical splicing machinery. Our results provide novel insights into the molecular regulation of GnRH splicing and highlight putrescine as a potential modulator of reproductive function through alternative splicing mechanisms.

01 Mar 2025·WIREs RNA

Functional Landscape of hnRNPA3 in Disease Pathogenesis

Review

Author: Li, Genghan ; Chen, Fang ; Zhang, Jihong ; Fu, Shuang

ABSTRACTThe heterogeneous nuclear ribonucleic acid protein family participates in various intracellular reactions, such as RNA splicing, transport, DNA repair, cellular signal transduction, and gene expression regulation, and is involved in various disease processes. As a late‐discovered member, heterogeneous nuclear ribonucleoprotein A3 has received increasing attention, but its main physiological functions and exact mechanisms involved in disease processes have not yet reached a consensus. In this review, we summarize the function of heterogeneous nuclear ribonucleoprotein A3 and the literature on its role in neurodegenerative and metabolic diseases, as well as in various tumors, to explore the applicability of heterogeneous nuclear ribonucleoprotein A3 as a therapeutic target and prognostic indicator.

01 Mar 2025·Poultry Science

Characterization and functional analysis of chicken hnRNP protein

Article

Author: Huang, Manzi ; Wu, Huansheng ; Wang, Ke ; Zeng, Qinghua

While the role of hnRNP proteins in modulating interferon signaling and virus replication in mammals has been extensively studied, the impact of chicken hnRNPs on innate immune response and Infectious Bursal Disease Virus (IBDV) replication remains largely unexplored. In this study, multiple chicken hnRNPs were identified to interact with genomic dsRNA. Initially, these hnRNPs were found to be exclusively localized in the nucleus before IBDV infection. However, post-infection, they translocated into the cytoplasm to co-localize with the viral dsRNA. Furthermore, the effects of various chicken hnRNPs on IFN-β activation, induced by the chicken MDA5-MAVS-TBK1 and STING-IRF7 pathway, were analyzed. Among these hnRNPs, hnRNPA3 demonstrated the most significant reduction in inhibiting IFN-β activation at the MAVS step. Additionally, overexpression of chicken hnRNPA3 was found to markedly enhance IBDV replication. Conversely, silencing chicken hnRNPA3 via siRNA significantly increased IFN-β production, thereby substantially suppressing IBDV replication. In summary, our findings reveal for the first time that multiple chicken hnRNPs interact with viral dsRNA, modulate IFN-β production, and specifically, that chicken hnRNPA3 promotes IBDV replication. These insights into the role of chicken hnRNPs in viral replication and immune response could pave the way for new therapeutic strategies against IBDV.

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HNRNPA3

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