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Arginine methylation reduces hnRNPA2 phase separation, disrupting arginine-mediated contacts. These results highlight the mechanistic role of specific LC domain interactions and modifications conserved across many hnRNP family members but altered by aggregation-causing pathological mutations.
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Moreover, SRSF10, hnRNP A1/A2 and Sam68 collaborate to drive the DNA damage-induced splicing response of several transcripts that produce components implicated in apoptosis, cell-cycle control and DNA repair.
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High HNRNPA2B1 expression is associated with cervical cancer.
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m6A switches may account for the previously seen enhanced hnRNP A2/B1 binding adjacent to m6A; instead of direct binding to m6A, m6A may promote accessibility of hnRNP A2/B1 to certain binding sites, thereby explaining how m6A can facilitate the ability of hnRNP A2/B1 to enhance nuclear events such as pri-miRNA processing
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revealed a novel heterozygous missense mutation of hnRNPA2B1 gene (c.929C>T, p. P310L) in the two patients which was then verified in all affected individuals
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Cilostazol pretreatment can reduce the excessive expression of inflammatory cytokines and chemokines and hnRNP A2/B1 by the Behcet's disease-related stimulants.
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UCP2 stimulates hnRNPA2/B1, GLUT1 and PKM2 expression and sensitizes pancreatic cancer cells to glycolysis inhibition.
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We demonstrate that the wild-type sequence harbors an hnRNP A1 and hnRNP A2/B1-binding exonic splicing silencer (ESS) overlapping the 5'splice site (5'ss) that prevents pseudoexon inclusion.we demonstrate that splice switching oligonucleotide (SSO) mediated blocking of the pseudoexon 3'ss and 5'ss effectively restores normal GLA splicing
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Data suggest that galectin-3 and heterogeneous ribonucleoprotein particle component hnRNPA2B1 interact as members of the early splicing machinery.
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effect of mutations on the aggregation propensity of hnRNPA2
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ALS-associated hnRNPA2B1 D290V mutant patient fibroblasts and motor neurons differentiated from iPSCs (iPSC-MNs) demonstrate abnormal splicing changes, likely due to increased nuclear-insoluble hnRNPA2B1. Mutant iPSC-MNs display decreased survival in long-term culture and exhibit hnRNPA2B1 localization to cytoplasmic granules as well as exacerbated changes in gene expression and splicing upon cellular stress.
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Motor-neuron disease (MND)-linked RNA-binding proteins (RBPs), TDP-43, FUS, and hnRNPA2B1, bind to and induce structural alteration of UGGAAexp. These RBPs suppress UGGAAexp-mediated toxicity in Drosophila by functioning as RNA chaperones for proper UGGAAexp folding and regulation of pentapeptide repeat translation.
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To examine the relationship between amino acid sequence and aggregation propensity, a diverse set of point mutations in the hnRNPA2B1 prion-like domain.
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We concluded that hnRNPA2B1 promotes the tumorigenic potential of breast cancer cells, MCF-7 and MDA-MB-231, through the extracellular-signal-regulated kinase 1/2 or signal transducer and activator of transcription 3 pathway, which may serve as a target for future therapies.
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results demonstrate that hnRNPA2/B1 promotes tumor cell growth by activating COX-2 signaling in NSCLC cells and imply that the hnRNPA2/B1/COX-2 pathway may be a potential therapeutic target for human lung cancers.
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Detection of hnRNP A2/B1 expression may be useful as a biomarker for prediction of glioma progression.
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The results indicate both genetic and physical interactions between disease-linked RNA-binding proteinss and DNAJB6/mrj, suggesting etiologic overlap between the pathogenesis of adult-onset inherited myopathies initiated by mutations in hnRNPA2B1 and DNAJB6.
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hnRNPA2B1, hnRNPD, hnRNPL , and YBX1 might play important roles in gastric cancer tumorigenesis.
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A unique role of the embryonic miR-369-HNRNPA2B1 axis in controlling metabolic enzyme function.
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lowering the levels of hnRNP A1/A2 elicits defective transcription elongation on a fraction of P-TEFb-dependent genes, hence favoring the transcription of P-TEFb-independent genes
