YTHDC2 (human, recombinant)

YTH domain containing 2 (YTHDC2) is an ATP-dependent 3’-5’ RNA helicase and a member of the DExD/H-box family of helicases.¹ YTHDC2 contains ATP binding, ATP hydrolysis, and RNA binding motifs.¹ The YTH domain binds to N⁶-methyladenosine-modified germline messenger RNA to regulate meiotic gene expression in mammalian germ cells, mediating the mitotic-to-meiotic transition in mouse germ cells.^2,3 Ythdc2^-/- male and female mice show disrupted meiotic prophase progression.³ Male Ythdc2^-/- mice have degraded germ cells and lack mature spermatozoa, while female Ythdc2^-/- mice lack developing ovarian follicles and have few germ cells. YTHDC2 also facilitates hepatitis C virus (HCV) genome replication by binding to the HCV replication cofactor cyclophilin B and the HCV RNA polymerase non-structural protein 5B (NS5B).⁴ YTHDC2 downregulation inhibits proliferation in Huh7 hepatocellular carcinoma cells and reduces metastasis a Y2KD-116 mouse xenograft model using HCT116 cells in which YTHDC2 is downregulated.^4,5 The expression of YTHDC2 in isolated human tumor tissue is positively correlated with tumor stage and lymph node metastasis.⁵

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1. Tanabe, A., Konno, J., Tanikawa, K., et al. Transcriptional machinery of TNF-α-inducible YTH domain containing 2 (YTHDC2) gene. Gene 535(1), 24-32 (2014).

2. Wojtas, M.N., Pandey, R.R., Mendel, M., et al. Regulation of m6A transcripts by the 3'→5' RNA helicase YTHDC2 is essential for a successful meiotic program in the mammalian germline. Mol. Cell 68(2), 374-387 (2017).

3. Bailey, A.S., Batista, P.J., Gold, R.S., et al. The conserved RNA helicase YTHDC2 regulates the transition from proliferation to differentiation in the germline. Elife pii:e26116, (2017).

4. Morohashi, K., Sahara, H., Watashi, K., et al. Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B. PLoS One 6(4):e18285, (2011).

5. Tanabe, A., Tanikawa, K., Tsunetomi, M., et al. RNA helicase YTHDC2 promotes cancer metastasis via the enhancement of the efficiency by which HIF-1α mRNA is translated. Cancer Lett. 376(1), 34-42 (2016).