WIG1 is crucial for AGO2-mediated ACOT7 mRNA silencing via miRNA-dependent and -independent mechanisms

RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified ACOT7 mRNA as a novel target of human WIG1. ACOT7 mRNA decay was triggered by the microRNA miR-9 in a WIG1-dependent manner via classic recruitment of Argonaute 2...

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Published in:Nucleic acids research Vol. 45; no. 11; pp. 6894 - 6910
Main Authors: Lee, Hyung Chul, Jung, Seung Hee, Hwang, Hyun Jung, Kang, Donghee, De, Supriyo, Dudekula, Dawood B., Martindale, Jennifer L., Park, Byungkyu, Park, Seung Kuk, Lee, Eun Kyung, Lee, Jeong-Hwa, Jeong, Sunjoo, Han, Kyungsook, Park, Heon Joo, Ko, Young-Gyu, Gorospe, Myriam, Lee, Jae-Seon
Format: Journal Article
Language:English
Published: England Oxford University Press 20.06.2017
Subjects:
3' Untranslated Regions
Argonaute Proteins - physiology
Base Sequence
Binding Sites
Carrier Proteins - physiology
Eukaryotic Initiation Factors - metabolism
HCT116 Cells
HEK293 Cells
Humans
Inverted Repeat Sequences
MCF-7 Cells
MicroRNAs - physiology
Nuclear Proteins - physiology
Protein Binding
Protein Biosynthesis
Protein Domains
RNA
RNA Interference
RNA Stability
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA-Binding Proteins
ISSN:0305-1048, 1362-4962, 1362-4962
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Abstract RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified ACOT7 mRNA as a novel target of human WIG1. ACOT7 mRNA decay was triggered by the microRNA miR-9 in a WIG1-dependent manner via classic recruitment of Argonaute 2 (AGO2). Interestingly, AGO2 was also recruited to ACOT7 mRNA in a WIG1-dependent manner in the absence of miR-9, which indicates an alternative model whereby WIG1 controls AGO2-mediated gene silencing. The WIG1-AGO2 complex attenuated translation initiation via an interaction with translation initiation factor 5B (eIF5B). These results were confirmed using a WIG1 tethering system based on the MS2 bacteriophage coat protein and a reporter construct containing an MS2-binding site, and by immunoprecipitation of WIG1 and detection of WIG1-associated proteins using liquid chromatography-tandem mass spectrometry. We also identified WIG1-binding motifs using photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation analyses. Altogether, our data indicate that WIG1 governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 to lower the stability of and suppress the translation of ACOT7 mRNA.
AbstractList RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified ACOT7 mRNA as a novel target of human WIG1. ACOT7 mRNA decay was triggered by the microRNA miR-9 in a WIG1-dependent manner via classic recruitment of Argonaute 2 (AGO2). Interestingly, AGO2 was also recruited to ACOT7 mRNA in a WIG1-dependent manner in the absence of miR-9, which indicates an alternative model whereby WIG1 controls AGO2-mediated gene silencing. The WIG1-AGO2 complex attenuated translation initiation via an interaction with translation initiation factor 5B (eIF5B). These results were confirmed using a WIG1 tethering system based on the MS2 bacteriophage coat protein and a reporter construct containing an MS2-binding site, and by immunoprecipitation of WIG1 and detection of WIG1-associated proteins using liquid chromatography-tandem mass spectrometry. We also identified WIG1-binding motifs using photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation analyses. Altogether, our data indicate that WIG1 governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 to lower the stability of and suppress the translation of ACOT7 mRNA.RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified ACOT7 mRNA as a novel target of human WIG1. ACOT7 mRNA decay was triggered by the microRNA miR-9 in a WIG1-dependent manner via classic recruitment of Argonaute 2 (AGO2). Interestingly, AGO2 was also recruited to ACOT7 mRNA in a WIG1-dependent manner in the absence of miR-9, which indicates an alternative model whereby WIG1 controls AGO2-mediated gene silencing. The WIG1-AGO2 complex attenuated translation initiation via an interaction with translation initiation factor 5B (eIF5B). These results were confirmed using a WIG1 tethering system based on the MS2 bacteriophage coat protein and a reporter construct containing an MS2-binding site, and by immunoprecipitation of WIG1 and detection of WIG1-associated proteins using liquid chromatography-tandem mass spectrometry. We also identified WIG1-binding motifs using photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation analyses. Altogether, our data indicate that WIG1 governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 to lower the stability of and suppress the translation of ACOT7 mRNA.
RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified ACOT7 mRNA as a novel target of human WIG1. ACOT7 mRNA decay was triggered by the microRNA miR-9 in a WIG1-dependent manner via classic recruitment of Argonaute 2 (AGO2). Interestingly, AGO2 was also recruited to ACOT7 mRNA in a WIG1-dependent manner in the absence of miR-9, which indicates an alternative model whereby WIG1 controls AGO2-mediated gene silencing. The WIG1–AGO2 complex attenuated translation initiation via an interaction with translation initiation factor 5B (eIF5B). These results were confirmed using a WIG1 tethering system based on the MS2 bacteriophage coat protein and a reporter construct containing an MS2-binding site, and by immunoprecipitation of WIG1 and detection of WIG1-associated proteins using liquid chromatography-tandem mass spectrometry. We also identified WIG1-binding motifs using photoactivatable ribonucleoside-enhanced crosslinking and immunoprecipitation analyses. Altogether, our data indicate that WIG1 governs the miRNA-dependent and the miRNA-independent recruitment of AGO2 to lower the stability of and suppress the translation of ACOT7 mRNA.
Author Park, Heon Joo
Lee, Jae-Seon
Lee, Eun Kyung
Gorospe, Myriam
Jeong, Sunjoo
Hwang, Hyun Jung
Dudekula, Dawood B.
De, Supriyo
Han, Kyungsook
Lee, Hyung Chul
Jung, Seung Hee
Ko, Young-Gyu
Park, Byungkyu
Lee, Jeong-Hwa
Martindale, Jennifer L.
Kang, Donghee
Park, Seung Kuk
AuthorAffiliation 2 Medical Research Center, Inha University College of Medicine, Incheon 22212, Korea
3 Laboratory of Genetics, National Institute on Aging-Intramural Research Program, NIH, Baltimore, MD 21224, USA
1 Department of Molecular Medicine, Medical Research Center, Inha University College of Medicine, Incheon 22212, Korea
6 Department of Biochemistry, College of Medicine, The Catholic University of Korea, Seoul 06591, Korea
4 Department of Computer Science and Engineering, Inha University, Incheon 22212, Korea
7 Department of Microbiology, Inha University College of Medicine, Incheon 22212, Korea
8 Division of Life Sciences, Korea University, Seoul 02841, Korea
5 Department of Molecular Biology, Dankook University, Yongin 16890, Korea
AuthorAffiliation_xml – name: 4 Department of Computer Science and Engineering, Inha University, Incheon 22212, Korea
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– name: 1 Department of Molecular Medicine, Medical Research Center, Inha University College of Medicine, Incheon 22212, Korea
– name: 6 Department of Biochemistry, College of Medicine, The Catholic University of Korea, Seoul 06591, Korea
– name: 8 Division of Life Sciences, Korea University, Seoul 02841, Korea
– name: 2 Medical Research Center, Inha University College of Medicine, Incheon 22212, Korea
– name: 7 Department of Microbiology, Inha University College of Medicine, Incheon 22212, Korea
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Snippet RNA-binding proteins (RBPs) are involved in mRNA splicing, maturation, transport, translation, storage and turnover. Here, we identified ACOT7 mRNA as a novel...
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StartPage 6894
SubjectTerms 3' Untranslated Regions
Argonaute Proteins - physiology
Base Sequence
Binding Sites
Carrier Proteins - physiology
Eukaryotic Initiation Factors - metabolism
HCT116 Cells
HEK293 Cells
Humans
Inverted Repeat Sequences
MCF-7 Cells
MicroRNAs - physiology
Nuclear Proteins - physiology
Protein Binding
Protein Biosynthesis
Protein Domains
RNA
RNA Interference
RNA Stability
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA-Binding Proteins
Title WIG1 is crucial for AGO2-mediated ACOT7 mRNA silencing via miRNA-dependent and -independent mechanisms
URI https://www.ncbi.nlm.nih.gov/pubmed/28472401
https://www.proquest.com/docview/1896042896
https://pubmed.ncbi.nlm.nih.gov/PMC5499809
Volume 45
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