ArticleThe Journal of biological chemistry2015
Molecular insights into the coding region determinant-binding protein-RNA interaction through site-directed mutagenesis in the heterogeneous nuclear ribonucleoprotein-K-homology domains.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- FUBL-3/FUBP1 mediates mitochondrial stress-induced chromatin remodeling and longevity.Science advances · 2026Article
- KH-R3H domain cooperation in RNA recognition by the global RNA-binding protein KhpB.Nature communications · 2025Article
- IGF2BP1 promotes multiple myeloma with chromosome 1q gain via increasing CDC5L expression in an mGenes & diseases · 2025Article
- IGF2BPs as novel mGenes & diseases · 2024Review
- A specific dispiropiperazine derivative that arrests cell cycle, induces apoptosis, necrosis and DNA damage.Scientific reports · 2023Article
- Article
- FMRP - G-quadruplex mRNA - miR-125a interactions: Implications for miR-125a mediated translation regulation of PSD-95 mRNA.PloS one · 2019Article
- Identification and Characterization of Sindbis Virus RNA-Host Protein Interactions.Journal of virology · 2018Article
- SRC IncreasesMolecular and cellular biology · 2018Article
- The DEAD-box protein DDX43 (HAGE) is a dual RNA-DNA helicase and has a K-homology domain required for full nucleic acid unwinding activity.The Journal of biological chemistry · 2017Article
- Article
- PCBP2 enables the cadicivirus IRES to exploit the function of a conserved GRNA tetraloop to enhance ribosomal initiation complex formation.Nucleic acids research · 2016Article
- The KH domain facilitates the substrate specificity and unwinding processivity of DDX43 helicase.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ability of its four heterogeneous nuclear RNP-K-homology (KH) domains to physically associate with oncogenic mRNAs is a major criterion for the function of the coding region determinant-binding protein (CRD-BP). However, the particular RNA-binding role of each of the KH domains remains largely unresolved. Here, we mutated the first glycine to an aspartate in the universally conserved GXXG motif of the KH domain as an approach to investigate their role. Our results show that mutation of a single GXXG motif generally had no effect on binding, but the mutation in any two KH domains, with the exception of the combination of KH3 and KH4 domains, completely abrogated RNA binding in vitro and significantly retarded granule formation in zebrafish embryos, suggesting that any combination of at least two KH domains cooperate in tandem to bind RNA efficiently. Interestingly, we found that any single point mutation in one of the four KH domains significantly impacted CRD-BP binding to mRNAs in HeLa cells, suggesting that the dynamics of the CRD-BP-mRNA interaction vary over time in vivo. Furthermore, our results suggest that different mRNAs bind preferentially to distinct CRD-BP KH domains. The novel insights revealed in this study have important implications on the understanding of the oncogenic mechanism of CRD-BP as well as in the future design of inhibitors against CRD-BP function.
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