ArticleScientific reports2017
Dual mechanisms regulate the nucleocytoplasmic localization of human DDX6.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
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- Me31B: a key repressor in germline regulation and beyond.Bioscience reports · 2024Review
- Mutational analysis of the functional motifs of the DEAD-box RNA helicase Me31B/DDX6 in Drosophila germline development.FEBS letters · 2023Article
- The Terminal Extensions of Dbp7 Influence Growth and 60S Ribosomal Subunit Biogenesis inInternational journal of molecular sciences · 2023Article
- RNA Helicase DDX6 Regulates A-to-I Editing and Neuronal Differentiation in Human Cells.International journal of molecular sciences · 2023Article
- A proteomics approach identifies novel resident zebrafish Balbiani body proteins Cirbpa and Cirbpb.Developmental biology · 2022Article
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- RNA Biology Provides New Therapeutic Targets for Human Disease.Frontiers in genetics · 2019Review
- Review
- Differential mMolecular cell · 2018Article
- The DEAD-box RNA-binding protein DDX6 regulates parental RNA decay for cellular reprogramming to pluripotency.PloS one · 2018Article
- DEAD-box helicase 6 (DDX6) is a new negative regulator for milk synthesis and proliferation of bovine mammary epithelial cells.In vitro cellular & developmental biology. Animal · 2018Article
- ALBA4 modulates its stage-specific interactions and specific mRNA fates during Plasmodium yoelii growth and transmission.Molecular microbiology · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DDX6 is a conserved DEAD-box protein (DBP) that plays central roles in cytoplasmic RNA regulation, including processing body (P-body) assembly, mRNA decapping, and translational repression. Beyond its cytoplasmic functions, DDX6 may also have nuclear functions because its orthologues are known to localize to nuclei in several biological contexts. However, it is unclear whether DDX6 is generally present in human cell nuclei, and the molecular mechanism underlying DDX6 subcellular distribution remains elusive. In this study, we showed that DDX6 is commonly present in the nuclei of human-derived cells. Our structural and molecular analyses deviate from the current model that the shuttling of DDX6 is directly mediated by the canonical nuclear localization signal (NLS) and nuclear export signal (NES), which are recognized and transported by Importin-α/β and CRM1, respectively. Instead, we show that DDX6 can be transported by 4E-T in a piggyback manner. Furthermore, we provide evidence for a novel nuclear targeting mechanism in which DDX6 enters the newly formed nuclei by "hitch-hiking" on mitotic chromosomes with its C-terminal domain during M phase progression. Together, our results indicate that the nucleocytoplasmic localization of DDX6 is regulated by these dual mechanisms.
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