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DDX3X is a substrate of both HDAC6 catalytic domains.DDX3X is acetylated under specific stress conditions.
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Mitogen-activated protein kinases and glycogen synthase kinase 3 phosphorylate Gle1A and thereby coordinate stress granule dynamics by altering DDX3 function.
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DDX3X is required for full CK1 activity in living cells. Phosphorylation by CK1 impairs the ATPase activity of DDX3X and RNA destabilizes the DDX3X-CK1 complex.
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the RNA helicase DDX3, is crucial in translation initiation of HIV-1 mRNA, but also fulfills an important role as RNA sensor and inducer of antiviral immunity in dendritic cells.
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Our genetic and functional data suggest that partial loss of function of DDX3X can cause syndromic ID. The p.R79K allele affects a region of the protein outside the critical RNA helicase domain, offering a credible explanation for the observed retention of partial function, viability in hemizygous males, and lack of pathology in females
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our study established DDX3 as a critical host interacting partner of the arenavirus nucleoprotein
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an N-terminal conserved Nuclear Export Signal (NES) is required for export of human DDX3 from the nucleus, and identified three regions within DDX3 that can independently facilitate its nuclear import.
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TRPV4 mediates Ca(2+) influx and nuclear accumulation of DDX3X in cells exposed to the Zika virus. Targeting of TRPV4 reduces infectivity of dengue, hepatitis C and Zika viruses. Our results highlight the role of TRPV4 in the regulation of DDX3X-dependent control of RNA metabolism and viral infectivity.
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DDX3 regulates MTP gene expression and lipid homeostasis through interplay with HNF4 and SHP.
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Through adopting the immunoprecipitation (IP), RNA immunoprecipitation (RIP), dual luciferase reporter assays, the authors illustrate that DDX3X could interact with Drosha/DGCR8 complex, elevate the processing activity of Drosha/DGCR8 complex on pri-miRNAs, and increase mature miRNA expression levels.
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our study suggested that DDX3 prevents generation of cancer stem cells through epigenetically regulating a subset of tumor-suppressive miRNAs expressions, which strengthens tumor suppressor role of DDX3 in hepatocellular carcinoma.
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this study shows that cancer-associated DDX3X mutations drive stress granule assembly and impair global translation
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we demonstrated that DDX3 modulated the activity of PP2A by controlling the phosphorylation of PP2A-C, which might enable PP2A-C to regulate NF-kappaB signal pathway by dephosphorylating IKK-beta.
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Data suggest that L protein from LCMV interactions with host proteome, specifically DDX3X, NKRF, and TRIM21. (LCMV = Lymphocytic choriomeningitis mammarenavirus; DDX3X = DEAD-box helicase 3; NKRF = NF-kappa-B-repressing factor; TRIM21 = tripartite motif-containing protein-21)
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DDX3 interacts extensively with RNA and ribosomal machinery to help remodel the translation landscape in response to stress, while cancer-related DDX3 variants adapt this response to selectively preserve translation
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Mechanistically, increased KRAS expression induced ROS production, which elevated HIF-1alpha and YAP1 expression. Increased HIF-1alpha persistently promoted DDX3 expression via a KRAS/ROS/HIF-1alpha feedback loop.
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Our study suggests that rottlerin exhibits its anti-cancer activity partly due to upregulation of DDX3 in hepatocellular carcinoma cells.
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DDX3 may play an oncogenic role to promote tumor growth and invasion in colon cancer cells
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data have demonstrated that Venezuelan equine encephalitis virus (VEEV)-nsP3 associates with DDX1 and DDX3 in infected cells to facilitate viral multiplication; determined that VEEV-nsP3 interacts with a pre-formed translational complex, comprising of DX3:eIF4A:eIF4G:PABP to potentially aid in translation of viral proteins.
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Data suggest that DEAD-box helicase 3 (DDX3X) physically interacts and co-localizes with poly(A)-binding cytoplasmic protein 1 (PABPC1) and caprin-1 in lamellipodia at the leading edge of spreading cells; these interactions are dependent on mRNA; depletion of DDX3X (via gene silencing with the CRISPR-Cas system) leads to decreased cell motility. These studies were conducted using MRC5 lung fibroblast cell line.
