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Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
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Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
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Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation

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Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
Journal Article

Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation

2018
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Overview
N 6 -methyladenosine (m 6 A) is the most prevalent modification in eukaryotic messenger RNAs (mRNAs) and is interpreted by its readers, such as YTH domain-containing proteins, to regulate mRNA fate. Here, we report the insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs; including IGF2BP1/2/3) as a distinct family of m 6 A readers that target thousands of mRNA transcripts through recognizing the consensus GG(m 6 A)C sequence. In contrast to the mRNA-decay-promoting function of YTH domain-containing family protein 2, IGF2BPs promote the stability and storage of their target mRNAs (for example, MYC ) in an m 6 A-dependent manner under normal and stress conditions and therefore affect gene expression output. Moreover, the K homology domains of IGF2BPs are required for their recognition of m 6 A and are critical for their oncogenic functions. Thus, our work reveals a different facet of the m 6 A-reading process that promotes mRNA stability and translation, and highlights the functional importance of IGF2BPs as m 6 A readers in post-transcriptional gene regulation and cancer biology. Huang et al. identify IGF2BPs as an additional class of N 6 -methyladenosine (m 6 A) reader proteins. They find that IGF2BPs selectively bind to m 6 A-containing mRNAs and promote their stability.