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| Home > Publications Database > Translational repression of the disintegrin and metalloprotease ADAM10 by a stable G-quadruplex secondary structure in its 5'-untranslated region. > print |
| 001 | 136395 | ||
| 005 | 20240321220048.0 | ||
| 024 | 7 | _ | |a 10.1074/jbc.M111.296921 |2 doi |
| 024 | 7 | _ | |a pmid:22065584 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC3248004 |2 pmc |
| 024 | 7 | _ | |a 0021-9258 |2 ISSN |
| 024 | 7 | _ | |a 1067-8816 |2 ISSN |
| 024 | 7 | _ | |a 1083-351X |2 ISSN |
| 037 | _ | _ | |a DZNE-2020-02717 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Lammich, Sven |0 P:(DE-HGF)0 |b 0 |e Corresponding author |
| 245 | _ | _ | |a Translational repression of the disintegrin and metalloprotease ADAM10 by a stable G-quadruplex secondary structure in its 5'-untranslated region. |
| 260 | _ | _ | |a Bethesda, Md. |c 2011 |b Soc.60645 |
| 264 | _ | 1 | |3 online |2 Crossref |b American Society for Biochemistry & Molecular Biology (ASBMB) |c 2011-11-07 |
| 264 | _ | 1 | |3 print |2 Crossref |b American Society for Biochemistry & Molecular Biology (ASBMB) |c 2011-12-30 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1586857862_30145 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Anti-amyloidogenic processing of the amyloid precursor protein APP by α-secretase prevents formation of the amyloid-β peptide, which accumulates in senile plaques of Alzheimer disease patients. α-Secretase belongs to the family of a disintegrin and metalloproteases (ADAMs), and ADAM10 is the primary candidate for this anti-amyloidogenic activity. We recently demonstrated that ADAM10 translation is repressed by its 5'-UTR and that in particular the first half of ADAM10 5'-UTR is responsible for translational repression. Here, we asked whether specific sequence motifs exist in the ADAM10 5'-UTR that are able to form complex secondary structures and thus potentially inhibit ADAM10 translation. Using circular dichroism spectroscopy, we demonstrate that a G-rich region between nucleotides 66 and 94 of the ADAM10 5'-UTR forms a highly stable, intramolecular, parallel G-quadruplex secondary structure under physiological conditions. Mutation of guanines in this sequence abrogates the formation of the G-quadruplex structure. Although the G-quadruplex structure efficiently inhibits translation of a luciferase reporter in in vitro translation assays and in living cells, inhibition of G-quadruplex formation fails to do so. Moreover, expression of ADAM10 was similarly repressed by the G-quadruplex. Mutation of the G-quadruplex motif results in a significant increase of ADAM10 levels and consequently APPsα secretion. Thus, we identified a critical RNA secondary structure within the 5'-UTR, which contributes to the translational repression of ADAM10. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a 5' Untranslated Regions |2 NLM Chemicals |
| 650 | _ | 7 | |a Membrane Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Amyloid Precursor Protein Secretases |0 EC 3.4.- |2 NLM Chemicals |
| 650 | _ | 7 | |a ADAM Proteins |0 EC 3.4.24.- |2 NLM Chemicals |
| 650 | _ | 7 | |a ADAM10 Protein |0 EC 3.4.24.81 |2 NLM Chemicals |
| 650 | _ | 7 | |a ADAM10 protein, human |0 EC 3.4.24.81 |2 NLM Chemicals |
| 650 | _ | 2 | |a 5' Untranslated Regions: physiology |2 MeSH |
| 650 | _ | 2 | |a ADAM Proteins: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a ADAM Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a ADAM10 Protein |2 MeSH |
| 650 | _ | 2 | |a Amyloid Precursor Protein Secretases: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Amyloid Precursor Protein Secretases: genetics |2 MeSH |
| 650 | _ | 2 | |a HEK293 Cells |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Membrane Proteins: biosynthesis |2 MeSH |
| 650 | _ | 2 | |a Membrane Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a Mutation |2 MeSH |
| 650 | _ | 2 | |a Nucleic Acid Conformation |2 MeSH |
| 650 | _ | 2 | |a Protein Biosynthesis: physiology |2 MeSH |
| 700 | 1 | _ | |a Kamp, Frits |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Wagner, Judith |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Nuscher, Brigitte |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Zilow, Sonja |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Ludwig, Ann-Katrin |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Willem, Michael |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Haass, Christian |0 P:(DE-2719)2202037 |b 7 |e Last author |
| 773 | 1 | 8 | |a 10.1074/jbc.m111.296921 |b : American Society for Biochemistry & Molecular Biology (ASBMB), 2011-11-07 |n 52 |p 45063-45072 |3 journal-article |2 Crossref |t Journal of Biological Chemistry |v 286 |y 2011 |x 0021-9258 |
| 773 | _ | _ | |a 10.1074/jbc.M111.296921 |g Vol. 286, no. 52, p. 45063 - 45072 |0 PERI:(DE-600)1474604-9 |n 52 |q 286:52<45063 - 45072 |p 45063-45072 |t The journal of biological chemistry |v 286 |y 2011 |x 0021-9258 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3248004 |
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| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 7 |6 P:(DE-2719)2202037 |
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