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000136395 0247_ $$2doi$$a10.1074/jbc.M111.296921
000136395 0247_ $$2pmid$$apmid:22065584
000136395 0247_ $$2pmc$$apmc:PMC3248004
000136395 0247_ $$2ISSN$$a0021-9258
000136395 0247_ $$2ISSN$$a1067-8816
000136395 0247_ $$2ISSN$$a1083-351X
000136395 037__ $$aDZNE-2020-02717
000136395 041__ $$aEnglish
000136395 082__ $$a540
000136395 1001_ $$0P:(DE-HGF)0$$aLammich, Sven$$b0$$eCorresponding author
000136395 245__ $$aTranslational repression of the disintegrin and metalloprotease ADAM10 by a stable G-quadruplex secondary structure in its 5'-untranslated region.
000136395 260__ $$aBethesda, Md.$$bSoc.60645$$c2011
000136395 264_1 $$2Crossref$$3online$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2011-11-07
000136395 264_1 $$2Crossref$$3print$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2011-12-30
000136395 3367_ $$2DRIVER$$aarticle
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000136395 3367_ $$2BibTeX$$aARTICLE
000136395 3367_ $$2ORCID$$aJOURNAL_ARTICLE
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000136395 520__ $$aAnti-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.
000136395 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000136395 588__ $$aDataset connected to CrossRef, PubMed,
000136395 650_7 $$2NLM Chemicals$$a5' Untranslated Regions
000136395 650_7 $$2NLM Chemicals$$aMembrane Proteins
000136395 650_7 $$0EC 3.4.-$$2NLM Chemicals$$aAmyloid Precursor Protein Secretases
000136395 650_7 $$0EC 3.4.24.-$$2NLM Chemicals$$aADAM Proteins
000136395 650_7 $$0EC 3.4.24.81$$2NLM Chemicals$$aADAM10 Protein
000136395 650_7 $$0EC 3.4.24.81$$2NLM Chemicals$$aADAM10 protein, human
000136395 650_2 $$2MeSH$$a5' Untranslated Regions: physiology
000136395 650_2 $$2MeSH$$aADAM Proteins: biosynthesis
000136395 650_2 $$2MeSH$$aADAM Proteins: genetics
000136395 650_2 $$2MeSH$$aADAM10 Protein
000136395 650_2 $$2MeSH$$aAmyloid Precursor Protein Secretases: biosynthesis
000136395 650_2 $$2MeSH$$aAmyloid Precursor Protein Secretases: genetics
000136395 650_2 $$2MeSH$$aHEK293 Cells
000136395 650_2 $$2MeSH$$aHumans
000136395 650_2 $$2MeSH$$aMembrane Proteins: biosynthesis
000136395 650_2 $$2MeSH$$aMembrane Proteins: genetics
000136395 650_2 $$2MeSH$$aMutation
000136395 650_2 $$2MeSH$$aNucleic Acid Conformation
000136395 650_2 $$2MeSH$$aProtein Biosynthesis: physiology
000136395 7001_ $$0P:(DE-HGF)0$$aKamp, Frits$$b1
000136395 7001_ $$0P:(DE-HGF)0$$aWagner, Judith$$b2
000136395 7001_ $$0P:(DE-HGF)0$$aNuscher, Brigitte$$b3
000136395 7001_ $$0P:(DE-HGF)0$$aZilow, Sonja$$b4
000136395 7001_ $$0P:(DE-HGF)0$$aLudwig, Ann-Katrin$$b5
000136395 7001_ $$0P:(DE-HGF)0$$aWillem, Michael$$b6
000136395 7001_ $$0P:(DE-2719)2202037$$aHaass, Christian$$b7$$eLast author
000136395 77318 $$2Crossref$$3journal-article$$a10.1074/jbc.m111.296921$$b : American Society for Biochemistry & Molecular Biology (ASBMB), 2011-11-07$$n52$$p45063-45072$$tJournal of Biological Chemistry$$v286$$x0021-9258$$y2011
000136395 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M111.296921$$gVol. 286, no. 52, p. 45063 - 45072$$n52$$p45063-45072$$q286:52<45063 - 45072$$tThe journal of biological chemistry$$v286$$x0021-9258$$y2011
000136395 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3248004
000136395 909CO $$ooai:pub.dzne.de:136395$$pVDB
000136395 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2202037$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b7$$kDZNE
000136395 9131_ $$0G:(DE-HGF)POF3-342$$1G:(DE-HGF)POF3-340$$2G:(DE-HGF)POF3-300$$aDE-HGF$$bForschungsbereich Gesundheit$$lErkrankungen des Nervensystems$$vDisease Mechanisms and Model Systems$$x0
000136395 9141_ $$y2011
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