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• W4290189425 abstract "Abstract N 6 -adenosine methylation (m 6 A) is the most abundant mRNA modification that controls gene expression through diverse mechanisms. m 6 A-dependent regulation of oncogenes and tumor suppressors indeed contribute to tumor development. However, the role of m 6 A-mediated gene regulation after drug treatment or resistance is poorly understood. Here, we report that m 6 A modification of mitogen-activated protein kinase 13 ( MAPK13 ) determines the sensitivity of cancer cells to the mechanistic target of rapamycin complex 1 (mTORC1)- targeting chemotherapeutic agent rapamycin. mTORC1 induces m 6 A modification of MAPK13 mRNA at its 3’ untranslated region (3’UTR) through methyltransferase-like 3 (METTL3)-METTL14-Wilms’ tumor 1-associating protein (WTAP) methyltransferase complex, thereby stimulating its mRNA degradation via an m 6 A reader protein YTH domain family protein 2 (YTHDF2). Rapamycin blunts this process and stabilizes MAPK13 . Unexpectedly, MAPK13 silencing suppresses cell growth and enhances rapamycin’s anti-cancer effects, suggesting that MAPK13 is an oncogenic gene activated by rapamycin via a feedback regulation. Together, our data indicate that rapamycin-mediated MAPK13 mRNA stabilization may confer drug resistance, and it can thus be a therapeutic target to sensitize cancer cells to rapamycin." @default.
• W4290189425 created "2022-08-07" @default.
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• W4290189425 date "2022-08-06" @default.
• W4290189425 modified "2023-09-27" @default.
• W4290189425 title "MAPK13 stabilization via m⁶A modification limits anti-cancer efficacy of rapamycin" @default.
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• W4290189425 doi "https://doi.org/10.1101/2022.08.05.502726" @default.
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