DEAD-box RNA Helicases in the Multistep Process of Tumor Metastasis

Overview

Journal Mol Biol Rep

Specialty Molecular Biology

Date 2024 Sep 22

PMID 39306810

Authors

Shan Li

Tianyu Feng

Hang Yuan

Qin Li

Gang Zhao

Kai Li

Affiliations

Soon will be listed here.

Abstract

RNA helicases constitute a large family of proteins that share a catalytic core with high structural similarity. DEAD-box (DDX) proteins belong to the largest RNA helicase subfamily, and DDX members have been implicated in all facets of RNA metabolism, from transcription to translation, miRNA maturation, and RNA delay and degradation. Interestingly, an increasing number of studies have suggested a relationship between DDX proteins and cancer initiation and progression. The expression levels of many DDX proteins are elevated in a majority of cancers, and recent studies have demonstrated that some DDX proteins have a potent positive effect on promoting the metastasis of malignant cells. Metastasis is a complex, multistep cascade process that includes local invasion, intravasation and survival in the circulation, arrest at a distant organ site, extravasation and metastatic colonization; here, we review this process and present the suggested functions and mechanisms of DDX family proteins in particular steps of the invasion‒metastasis cascade.

References

Linder P, Jankowsky E . From unwinding to clamping - the DEAD box RNA helicase family. Nat Rev Mol Cell Biol. 2011; 12(8):505-16. DOI: 10.1038/nrm3154. View

Koltowska K, Okuda K, Gloger M, Rondon-Galeano M, Mason E, Xuan J . The RNA helicase Ddx21 controls Vegfc-driven developmental lymphangiogenesis by balancing endothelial cell ribosome biogenesis and p53 function. Nat Cell Biol. 2021; 23(11):1136-1147. DOI: 10.1038/s41556-021-00784-w. View

Burns W, Bird L, Heron D, Keren B, Ramachandra D, Thiffault I . Syndromic neurodevelopmental disorder associated with de novo variants in DDX23. Am J Med Genet A. 2021; 185(10):2863-2872. DOI: 10.1002/ajmg.a.62359. View

Galarza-Munoz G, Briggs F, Evsyukova I, Schott-Lerner G, Kennedy E, Nyanhete T . Human Epistatic Interaction Controls IL7R Splicing and Increases Multiple Sclerosis Risk. Cell. 2017; 169(1):72-84.e13. PMC: 5456452. DOI: 10.1016/j.cell.2017.03.007. View

Cargill M, Venkataraman R, Lee S . DEAD-Box RNA Helicases and Genome Stability. Genes (Basel). 2021; 12(10). PMC: 8535883. DOI: 10.3390/genes12101471. View

Zhang X, Tomar N, Kandel S, Audi S, Cowley Jr A, Dash R . Substrate- and Calcium-Dependent Differential Regulation of Mitochondrial Oxidative Phosphorylation and Energy Production in the Heart and Kidney. Cells. 2022; 11(1). PMC: 8750792. DOI: 10.3390/cells11010131. View

Li K, Mo C, Gong D, Chen Y, Huang Z, Li Y . DDX17 nucleocytoplasmic shuttling promotes acquired gefitinib resistance in non-small cell lung cancer cells via activation of β-catenin. Cancer Lett. 2017; 400:194-202. DOI: 10.1016/j.canlet.2017.02.029. View

10.

Valastyan S, Weinberg R . Tumor metastasis: molecular insights and evolving paradigms. Cell. 2011; 147(2):275-92. PMC: 3261217. DOI: 10.1016/j.cell.2011.09.024. View

11.

Steeg P . Targeting metastasis. Nat Rev Cancer. 2016; 16(4):201-18. PMC: 7055530. DOI: 10.1038/nrc.2016.25. View

12.

Welch D, Hurst D . Defining the Hallmarks of Metastasis. Cancer Res. 2019; 79(12):3011-3027. PMC: 6571042. DOI: 10.1158/0008-5472.CAN-19-0458. View

13.

Bakir B, Chiarella A, Pitarresi J, Rustgi A . EMT, MET, Plasticity, and Tumor Metastasis. Trends Cell Biol. 2020; 30(10):764-776. PMC: 7647095. DOI: 10.1016/j.tcb.2020.07.003. View

14.

Li D, Tian Y, Yin C, Huai Y, Zhao Y, Su P . Silencing of lncRNA Promotes Osteoblast Differentiation and Bone Formation via β-Catenin/TCF1/Runx2 Signaling Axis. Int J Mol Sci. 2019; 20(24). PMC: 6941011. DOI: 10.3390/ijms20246229. View

15.

Gonzalez D, Medici D . Signaling mechanisms of the epithelial-mesenchymal transition. Sci Signal. 2014; 7(344):re8. PMC: 4372086. DOI: 10.1126/scisignal.2005189. View

16.

Hamidi H, Ivaska J . Every step of the way: integrins in cancer progression and metastasis. Nat Rev Cancer. 2018; 18(9):533-548. PMC: 6629548. DOI: 10.1038/s41568-018-0038-z. View

17.

Moreno-Layseca P, Icha J, Hamidi H, Ivaska J . Integrin trafficking in cells and tissues. Nat Cell Biol. 2019; 21(2):122-132. PMC: 6597357. DOI: 10.1038/s41556-018-0223-z. View

18.

Dereeper A, Guignon V, Blanc G, Audic S, Buffet S, Chevenet F . Phylogeny.fr: robust phylogenetic analysis for the non-specialist. Nucleic Acids Res. 2008; 36(Web Server issue):W465-9. PMC: 2447785. DOI: 10.1093/nar/gkn180. View

19.

Jankowsky E . RNA helicases at work: binding and rearranging. Trends Biochem Sci. 2010; 36(1):19-29. PMC: 3017212. DOI: 10.1016/j.tibs.2010.07.008. View

20.

Jarmoskaite I, Russell R . DEAD-box proteins as RNA helicases and chaperones. Wiley Interdiscip Rev RNA. 2011; 2(1):135-52. PMC: 3032546. DOI: 10.1002/wrna.50. View

21.

Andreou A, Klostermeier D . The DEAD-box helicase eIF4A: paradigm or the odd one out?. RNA Biol. 2012; 10(1):19-32. PMC: 3590233. DOI: 10.4161/rna.21966. View

22.

Andersen C, Ballut L, Johansen J, Chamieh H, Nielsen K, Oliveira C . Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. Science. 2006; 313(5795):1968-72. DOI: 10.1126/science.1131981. View