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Translational regulation of Chk1 expression by eIF3a via interaction with the RNA-binding protein HuR
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In: Biochem J (2020)
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Abstract:
eIF3a is a putative subunit of the eukaryotic translation initiation factor 3 complex. Accumulating evidence suggests that eIF3a may have a translational regulatory function by suppressing translation of a subset of mRNAs while accelerating that of other mRNAs. Albeit the suppression of mRNA translation may derive from eIF3a binding to the 5′-UTRs of target mRNAs, how eIF3a may accelerate mRNA translation remains unknown. In this study, we show that eIF3a up-regulates translation of Chk1 but not Chk2 mRNA by interacting with HuR, which binds directly to the 3′-UTR of Chk1 mRNA. The interaction between eIF3a and HuR occurs at the 10-amino-acid repeat domain of eIF3a and the RNA recognition motif domain of HuR. This interaction may effectively circularize Chk1 mRNA to form an end-to-end complex that has recently been suggested to accelerate mRNA translation. Together with previous findings, we conclude that eIF3a may regulate mRNA translation by directly binding to the 5′-UTR to suppress or by interacting with RNA-binding proteins at 3′-UTRs to accelerate mRNA translation.
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Article
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URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8247610/
https://doi.org/10.1042/BCJ20200025
http://www.ncbi.nlm.nih.gov/pubmed/32391557
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Introduction of Western Ideology During the Late Ming and Early Qing
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In: Cross-Cultural Communication; Vol 13, No 10 (2017): Cross-Cultural Communication; 6-9 ; 1923-6700 ; 1712-8358 (2017)
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