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APP levels then decrease progressively as a function of age in close relationship with the gradual normalization of FMRP and hnRNP C levels.
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Endoplasmic reticulum resident chaperone GRP78, mitochondrial protein Prohibitin and heterogeneous nuclear ribonucleoprotein hnRNPC (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection.
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Our results indicate that a balance between lncRNA SNHG1 and hnRNPC regulates p53 activity and p53-dependent apoptosis upon doxorubicin treatment, and further indicate that a change in lncRNA subcellular localization under specific circumstances is biologically significant.
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These data suggest an interplay between CELF2 and hnRNP C as the mechanistic basis for activation-dependent alternative splicing of TRAF3 exon 8.
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These data indicate that hnRNPC1/C2 binds to both DNA and RNA and influences both gene expression and RNA splicing, but these actions do not appear to be linked through 1,25(OH)2D-mediated induction of transcription.
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These findings suggest that hnRNP C1/C2 is involved in dengue virus replication at the stage of viral RNA synthesis.
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HnRNP C, YB-1 and hnRNP L coordinately enhance skipping of human MUSK exon 10 to generate a Wnt-insensitive MuSK isoform.
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Our results suggested that hnRNP C1 controls HPV16 late gene expression.
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m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation
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PTBP1 and hnRNP C repress exon 3 inclusion, and that downregulation of PTBP1 inhibited BIM-mediated apoptosis.
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down-regulation of MALAT-1 expression compromised the cytoplasmic translocation of hnRNP C in the G2/M phase and resulted in G2/M arrest
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Heterogeneous nuclear ribonucleoprotein C is a key regulator of BRCA gene expression and homologous recombination-based DNA repair.
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By preventing U2AF65 binding to Alu elements, hnRNP C plays a critical role as a genome-wide sentinel protecting the transcriptome.
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The data indicated that hnRNPC controls the aggressiveness of glioblastoma cells through the regulation of PDCD4. Silencing of hnRNPC lowered miR-21 levels, in turn increasing the expression of PDCD4, suppressing Akt and p70S6K activation.
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p27kip1 upregulated by hnRNPC1/2 antagonizes CagA-mediated pathogenesis.
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study shows mechanism by which Pol II transcripts are classified according to length; heterotetramer of hnRNP C1/C2 measures the length of the transcripts like a molecular ruler, by binding to unstructured RNA regions longer than 200 to 300 nucleotides
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One of the identified proteins, hnRNPC, was found to interact with small hepatitis delta virus antigen in vitro and in vivo in human liver cells.
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Studies indicated that DDX21, HNRNPC, and RCC2 were isolated from Ku86 multicomponent complex in response to DNA damage.
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HNRNP C recognizes uridine tracts with a defined long-range spacing consistent with HNRNP particle organization.
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FMRP represses translation by recruiting APP mRNA to processing bodies, whereas hnRNP C promotes APP translation by displacing FMRP, thereby relieving the translational block.
