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eIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5'UTR
Choe, Junho, Ryu, Incheol, Park, Ok Hyun, Park, Joori, Cho, Hana, Yoo, Jin Seon, Chi, Sung Wook, Kim, Min Kyung, Song, Hyun Kyu, Kim, Yoon Ki
Proceedings of the National Academy of Sciences of the United States of America, 28 October 2014, Vol.111(43), pp.E4577-86 [Peer Reviewed Journal]

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The mRNP remodeling mediated by UPF1 promotes rapid degradation of replication-dependent histone mRNA
Choe, Junho, Ahn, Sang Ho, Kim, Yoon Ki
Nucleic acids research, August 2014, Vol.42(14), pp.9334-49 [Peer Reviewed Journal]

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Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g
Choe, Junho, Oh, Nara, Park, Sungjin, Lee, Ye Kyung, Song, Ok-Kyu, Locker, Nicolas, Chi, Sung-Gil, Kim, Yoon Ki
The Journal of biological chemistry, 25 May 2012, Vol.287(22), pp.18500-9 [Peer Reviewed Journal]
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Title: Translation initiation on mRNAs bound by nuclear cap-binding protein complex CBP80/20 requires interaction between CBP80/20-dependent translation initiation factor and eukaryotic translation initiation factor 3g
Author: Choe, Junho; Oh, Nara; Park, Sungjin; Lee, Ye Kyung; Song, Ok-Kyu; Locker, Nicolas; Chi, Sung-Gil; Kim, Yoon Ki
Subject: Protein Biosynthesis ; Eukaryotic Initiation Factor-3 -- Metabolism ; Nuclear Cap-Binding Protein Complex -- Metabolism ; RNA, Messenger -- Genetics
Description: In the cytoplasm of mammalian cells, either cap-binding proteins 80 and 20 (CBP80/20) or eukaryotic translation initiation factor (eIF) 4E can direct the initiation of translation. Although the recruitment of ribosomes to mRNAs during eIF4E-dependent translation (ET) is well characterized, the molecular mechanism for CBP80/20-dependent translation (CT) remains obscure. Here, we show that CBP80/20-dependent translation initiation factor (CTIF), which has been shown to be preferentially involved in CT but not ET, specifically interacts with eIF3g, a component of the eIF3 complex involved in ribosome recruitment. By interacting with eIF3g, CTIF serves as an adaptor protein to bridge the CBP80/20 and the eIF3 complex, leading to efficient ribosome recruitment during CT. Accordingly, down-regulation of CTIF using a small interfering RNA causes a redistribution of CBP80 from polysome fractions to subpolysome fractions, without significant consequence to eIF4E distribution. In addition, down-regulation...
Is part of: The Journal of biological chemistry, 25 May 2012, Vol.287(22), pp.18500-9
Identifier: 1083-351X (E-ISSN); 22493286 Version (PMID); 10.1074/jbc.M111.327528 (DOI)

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Ago2/miRISC-mediated inhibition of CBP80/20-dependent translation and thereby abrogation of nonsense-mediated mRNA decay require the cap-associating activity of Ago2
Choe, Junho, Cho, Hana, Chi, Sung-Gil, Kim, Yoon Ki
FEBS letters, 02 September 2011, Vol.585(17), pp.2682-7 [Peer Reviewed Journal]
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Title: Ago2/miRISC-mediated inhibition of CBP80/20-dependent translation and thereby abrogation of nonsense-mediated mRNA decay require the cap-associating activity of Ago2
Author: Choe, Junho; Cho, Hana; Chi, Sung-Gil; Kim, Yoon Ki
Subject: Eukaryotic Initiation Factor-2 -- Metabolism ; Nuclear Cap-Binding Protein Complex -- Metabolism ; RNA Stability -- Genetics
Description: Nuclear cap-binding protein (CBP) 80/20-dependent translation (CT) is one of the targets for miRNA-mediated gene silencing. Here, we provide evidence that human argonaute 2 (Ago2) competes with CBP80/20 for cap-association, inhibiting CT and thus nonsense-mediated mRNA decay (NMD), which is tightly coupled to CT. Tethering of Ago2, but not of Ago2F2V2 which lacks cap-association activity, to the 3'UTR of PTC-containing mRNA abrogates NMD. Immunoprecipitation using CBP80 antibody reveals that Ago2, but not Ago2F2V2, inhibits the binding of CBP80/20 to cap structure. Our observations provide molecular insight into the cross-talk between miRNA-mediated gene silencing, CT, and NMD.
Is part of: FEBS letters, 02 September 2011, Vol.585(17), pp.2682-7
Identifier: 1873-3468 (E-ISSN); 21840310 Version (PMID); 10.1016/j.febslet.2011.07.047 (DOI)

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The m(6)A Methyltransferase METTL3 Promotes Translation in Human Cancer Cells
Lin, Shuibin, Choe, Junho, Du, Peng, Triboulet, Robinson, Gregory, Richard I
Molecular cell, 05 May 2016, Vol.62(3), pp.335-345 [Peer Reviewed Journal]
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Title: The m(6)A Methyltransferase METTL3 Promotes Translation in Human Cancer Cells
Author: Lin, Shuibin; Choe, Junho; Du, Peng; Triboulet, Robinson; Gregory, Richard I
Subject: Egfr ; Mettl3 ; N(6)-Methyladenosine ; Cancer ; M(6)A ; Ribosome ; Translation ; Peptide Chain Initiation, Translational ; Adenocarcinoma -- Enzymology ; Lung Neoplasms -- Enzymology ; Methyltransferases -- Metabolism ; RNA, Messenger -- Metabolism
Description: METTL3 is an RNA methyltransferase implicated in mRNA biogenesis, decay, and translation control through N(6)-methyladenosine (m(6)A) modification. Here we find that METTL3 promotes translation of certain mRNAs including epidermal growth factor receptor (EGFR) and the Hippo pathway effector TAZ in human cancer cells. In contrast to current models that invoke m(6)A reader proteins downstream of nuclear METTL3, we find METTL3 associates with ribosomes and promotes translation in the cytoplasm. METTL3 depletion inhibits translation, and both wild-type and catalytically inactive METTL3 promote translation when tethered to a reporter mRNA. Mechanistically, METTL3 enhances mRNA translation through an interaction with the translation initiation machinery. METTL3 expression is elevated in lung adenocarcinoma and using both loss- and gain-of-function studies, we find that METTL3 promotes growth, survival, and invasion of human lung cancer cells. Our results uncover an important role of METTL3 in...
Is part of: Molecular cell, 05 May 2016, Vol.62(3), pp.335-345
Identifier: 1097-4164 (E-ISSN); 27117702 Version (PMID); 10.1016/j.molcel.2016.03.021 (DOI)

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SMG5-PNRC2 is functionally dominant compared with SMG5-SMG7 in mammalian nonsense-mediated mRNA decay
Cho, Hana, Han, Sisu, Choe, Junho, Park, Seung Gu, Choi, Sun Shim, Kim, Yoon Ki
Nucleic acids research, January 2013, Vol.41(2), pp.1319-28 [Peer Reviewed Journal]
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Title: SMG5-PNRC2 is functionally dominant compared with SMG5-SMG7 in mammalian nonsense-mediated mRNA decay
Author: Cho, Hana; Han, Sisu; Choe, Junho; Park, Seung Gu; Choi, Sun Shim; Kim, Yoon Ki
Subject: Nonsense Mediated Mrna Decay ; Carrier Proteins -- Metabolism ; Receptors, Cytoplasmic and Nuclear -- Metabolism ; Trans-Activators -- Metabolism
Description: In mammals, nonsense-mediated mRNA decay (NMD) functions in post-transcriptional gene regulation as well as mRNA surveillance. A key NMD factor, Upf1, becomes hyperphosphorylated by SMG1 kinase during the recognition of NMD substrates. Hyperphosphorylated Upf1 interacts with several factors including SMG5, SMG6, SMG7 and PNRC2 to trigger rapid mRNA degradation. However, the possible cross-talk among these factors and their selective use during NMD remain unknown. Here, we show that PNRC2 is preferentially complexed with SMG5, but not with SMG6 or SMG7, and that downregulation of PNRC2 abolishes the interaction between SMG5 and Dcp1a, a component of the decapping complex. In addition, tethering experiments reveal the function of Upf1, SMG5 and PNRC2 at the same step of NMD and the requirement of SMG6 for Upf1 for efficient mRNA degradation. Intriguingly, microarray results reveal the significant overlap of SMG5-dependent NMD substrates more with PNRC2-dependent NMD substrates than with SMG7-dependent...
Is part of: Nucleic acids research, January 2013, Vol.41(2), pp.1319-28
Identifier: 1362-4962 (E-ISSN); 23234702 Version (PMID); 10.1093/nar/gks1222 (DOI)

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Mettl1/Wdr4-Mediated mG tRNA Methylome Is Required for Normal mRNA Translation and Embryonic Stem Cell Self-Renewal and Differentiation
Lin, Shuibin, Liu, Qi, Lelyveld, Victor S, Choe, Junho, Szostak, Jack W, Gregory, Richard I
Molecular cell, 19 July 2018, Vol.71(2), pp.244-255.e5 [Peer Reviewed Journal]
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Title: Mettl1/Wdr4-Mediated mG tRNA Methylome Is Required for Normal mRNA Translation and Embryonic Stem Cell Self-Renewal and Differentiation
Author: Lin, Shuibin; Liu, Qi; Lelyveld, Victor S; Choe, Junho; Szostak, Jack W; Gregory, Richard I
Subject: Merip-Seq ; Mettl1 ; N(7)-Methylguanosine ; RNA Methylation ; Trac-Seq ; Wdr4 ; Embryonic Stem Cells ; M(7)G ; Neural Development ; Trna ; Translation ; Gtp-Binding Proteins -- Genetics ; Guanosine -- Analogs & Derivatives ; Methyltransferases -- Genetics ; RNA, Transfer -- Genetics
Description: tRNAs are subject to numerous modifications, including methylation. Mutations in the human N-methylguanosine (mG) methyltransferase complex METTL1/WDR4 cause primordial dwarfism and brain malformation, yet the molecular and cellular function in mammals is not well understood. We developed mG methylated tRNA immunoprecipitation sequencing (MeRIP-seq) and tRNA reduction and cleavage sequencing (TRAC-seq) to reveal the mG tRNA methylome in mouse embryonic stem cells (mESCs). A subset of 22 tRNAs is modified at a "RAGGU" motif within the variable loop. We observe increased ribosome occupancy at the corresponding codons in Mettl1 knockout mESCs, implying widespread effects on tRNA function, ribosome pausing, and mRNA translation. Translation of cell cycle genes and those associated with brain abnormalities is particularly affected. Mettl1 or Wdr4 knockout mESCs display defective self-renewal and neural differentiation. Our study uncovers the complexity of the mammalian mG tRNA methylome and...
Is part of: Molecular cell, 19 July 2018, Vol.71(2), pp.244-255.e5
Identifier: 1097-4164 (E-ISSN); 29983320 Version (PMID); 10.1016/j.molcel.2018.06.001 (DOI)

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microRNA/Argonaute 2 regulates nonsense-mediated messenger RNA decay
Choe, Junho, Cho, Hana, Lee, Hyung Chul, Kim, Yoon Ki
EMBO reports, May 2010, Vol.11(5), pp.380-6 [Peer Reviewed Journal]
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Title: microRNA/Argonaute 2 regulates nonsense-mediated messenger RNA decay
Author: Choe, Junho; Cho, Hana; Lee, Hyung Chul; Kim, Yoon Ki
Subject: Codon, Nonsense -- Genetics ; Eukaryotic Initiation Factor-2 -- Metabolism ; Micrornas -- Metabolism ; RNA Stability -- Genetics
Description: Imperfect base-pairing between microRNA (miRNA) and the 3'-untranslated region of target messenger RNA (mRNA) triggers translational repression of the target mRNA. Here, we provide evidence that human Argonaute 2 targets cap-binding protein (CBP)80/20-bound mRNAs and exon junction complex-bound mRNAs and inhibits nonsense-mediated mRNA decay (NMD), which is restricted tightly to CBP80/20-bound mRNAs. Furthermore, microarray analyses reveal that a subset of cellular transcripts, which are expected to be targeted for NMD, is stabilized by miRNA-mediated gene silencing. The regulation of NMD by miRNAs will shed light on a new post-transcriptional regulation mechanism of gene expression in mammalian cells.
Is part of: EMBO reports, May 2010, Vol.11(5), pp.380-6
Identifier: 1469-3178 (E-ISSN); 20395958 Version (PMID); 10.1038/embor.2010.44 (DOI)

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Nonsense-mediated translational repression involves exon junction complex downstream of premature translation termination codon
Lee, Hyung Chul, Oh, Nara, Cho, Hana, Choe, Junho, Kim, Yoon Ki
FEBS letters, 19 February 2010, Vol.584(4), pp.795-800 [Peer Reviewed Journal]
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Title: Nonsense-mediated translational repression involves exon junction complex downstream of premature translation termination codon
Author: Lee, Hyung Chul; Oh, Nara; Cho, Hana; Choe, Junho; Kim, Yoon Ki
Subject: Codon, Nonsense -- Genetics ; Exons -- Genetics ; Protein Biosynthesis -- Genetics ; Protein-Serine-Threonine Kinases -- Genetics ; Receptors, Transforming Growth Factor Beta -- Genetics
Description: Human transforming growth factor-beta receptor type 2 (TGFbetaR2) mRNA harboring a premature translation termination codon (PTC) generated by frameshift mutation is targeted for nonsense-mediated translational repression (NMTR), rather than nonsense-mediated mRNA decay (NMD). Here we show that exon junction complex (EJC) downstream of a PTC plays an inhibitory role in translation of TGFbetaR2 mRNA. Translational repression by core EJC components occurs after formation of 80S ribosome complex, which is demonstrated using different types of internal ribosome entry sites (IRESes). Our findings implicate EJCs or core EJC components as negative regulators of translation.
Is part of: FEBS letters, 19 February 2010, Vol.584(4), pp.795-800
Identifier: 1873-3468 (E-ISSN); 20067791 Version (PMID); 10.1016/j.febslet.2010.01.003 (DOI)

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Pioneer round of translation mediated by nuclear cap-binding proteins CBP80/20 occurs during prolonged hypoxia
Oh, Nara, Kim, Kyoung Mi, Choe, Junho, Kim, Yoon Ki
FEBS letters, 30 October 2007, Vol.581(26), pp.5158-64 [Peer Reviewed Journal]
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Title: Pioneer round of translation mediated by nuclear cap-binding proteins CBP80/20 occurs during prolonged hypoxia
Author: Oh, Nara; Kim, Kyoung Mi; Choe, Junho; Kim, Yoon Ki
Subject: RNA Stability ; Nuclear Cap-Binding Protein Complex -- Metabolism ; Protein Biosynthesis -- Genetics ; RNA, Messenger -- Metabolism
Description: Nonsense-mediated mRNA decay (NMD) is one of the mRNA surveillance mechanisms, which eliminates aberrant mRNAs harboring premature termination codons. NMD targets only mRNAs bound by the nuclear cap-binding protein complex CBP80/20 which directs the pioneer round of translation. Here we demonstrate that NMD occurs efficiently during prolonged hypoxia in which steady-state translation is drastically inhibited. Accordingly, CBP80 remains in the nucleus, and processing bodies are unaffected with regard to their abundance and number under prolonged hypoxic conditions. These results indicate that mRNAs enter the pioneer round of translation during prolonged hypoxia.
Is part of: FEBS letters, 30 October 2007, Vol.581(26), pp.5158-64
Identifier: 0014-5793 (ISSN); 17942097 Version (PMID)

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eIF4AIII enhances translation of nuclear cap-binding complex-bound mRNAs by promoting disruption of secondary structures in 5'UTR

The mRNP remodeling mediated by UPF1 promotes rapid degradation of replication-dependent histone mRNA