Heterogeneous nuclear ribonucleoproteins (hnRNPs) are a group of RNA-binding proteins with important roles in multiple aspects of nucleic acid metabolism, including the packaging of nascent transcripts, alternative splicing, transactivation of gene expression, and regulation of protein translation. As a core component of the hnRNP complex in mammalian cells, heterogeneous nuclear ribonucleoprotein A2B1 (hnRNP A2B1) participates in and coordinates various molecular events. Given its regulatory role in inflammation and cancer progression, hnRNP A2B1 has become a novel player in immune response, inflammation, and cancer development. Concomitant with these new roles, a surprising number of mechanisms deemed to regulate hnRNP A2B1 functions have been identified, including post-translational modifications, changes in subcellular localization, direct interactions with multiple DNAs, RNAs, and proteins or the formation of complexes with them, which have gradually made hnRNP A2B1 a molecular target for multiple drugs. In light of the rising interest in the intersection between cancer and inflammation, this review will focus on recent knowledge of the biological roles of hnRNP A2B1 in cancer, immune response, and inflammation.
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http://dx.doi.org/10.1016/j.ijbiomac.2022.09.104 | DOI Listing |
Biochim Biophys Acta Mol Basis Dis
January 2025
The Key Laboratory of Advanced Interdisciplinary Studies, Institute for Chemical Carcinogenesis, School of Public Health, Guangzhou Medical University, 1 Xinzao Road, Panyu District, Guangzhou 511436, PR China. Electronic address:
Heterogeneous nuclear ribonucleoprotein A2B1 (HNRNPA2B1), a member of the A/B subfamily of hnRNPs, plays a critical role in tumorigenesis, yet its expression patterns, molecular mechanisms, and prognostic significance remain inadequately characterized. In this study, we performed a comprehensive pan-cancer analysis utilizing multiple public databases, revealing that HNRNPA2B1 is consistently overexpressed in most tumor types and correlates with poor prognosis across several malignancies. Pathway enrichment analysis highlighted its involvement in RNA alternative splicing, transport, and stability, processes that contribute to tumor progression.
View Article and Find Full Text PDFNat Commun
December 2024
Department of Biochemistry, McGill University, Montreal, QC, Canada.
Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. Using high-resolution fluorescence microscopy, we discover that hippocampal and spinal cord motor neurons of mouse and human origin localize a subset of chaperone mRNAs to their dendrites and use microtubule-based transport to increase this asymmetric localization following proteotoxic stress.
View Article and Find Full Text PDFBrain Pathol
October 2024
Brain and Mind Centre and School of Medical Sciences, University of Sydney, Camperdown, New South Wales, Australia.
J Virol
September 2024
International Joint Research Center of National Animal Immunology, College of Veterinary Medicine, Henan Agricultural University, Zhengzhou, China.
Unlabelled: Viruses deploy sophisticated strategies to hijack the host's translation machinery to favor viral protein synthesis and counteract innate cellular defenses. However, little is known about the mechanisms by which Senecavirus A (SVA) controls the host's translation. Using a series of sophisticated molecular cell manipulation techniques, heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) was identified as an essential host factor involved in translation control in SVA-infected cells.
View Article and Find Full Text PDFMicrobiol Spectr
October 2024
State Key Laboratory of Virology, School of Public Health, Wuhan University, Wuhan, China.
The heterogeneous nuclear ribonucleoprotein (hnRNP A2B1) is a key component of the hnRNP complex involving RNA modulation in eukaryotic cells and it has also been reported to be involved in the replication of the hepatitis E virus, influenza A virus, and hepatitis B virus. However, it is not clear whether the role of the hnRNP A2B1 in viral replication is conserved among RNA viruses and what is the mechanism of hnRNP A2B1 in RNA virus replication. In this study, we first used severe fever with thrombocytopenia syndrome virus (SFTSV), a tick-borne RNA virus that causes a severe viral hemorrhagic fever as well as other RNA viruses including VSV-GFP, SeV, EV71, and ZIKV to demonstrate that knockout hnRNPA2B1 gene inhibited viral RNA replication and overexpression of hnRNP A2B1 could restore the RNA levels of all tested RNA viruses.
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