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000136438 0247_ $$2doi$$a10.1074/jbc.M111.328104
000136438 0247_ $$2pmid$$apmid:22194595
000136438 0247_ $$2pmc$$apmc:PMC3281599
000136438 0247_ $$2ISSN$$a0021-9258
000136438 0247_ $$2ISSN$$a1067-8816
000136438 0247_ $$2ISSN$$a1083-351X
000136438 037__ $$aDZNE-2020-02760
000136438 041__ $$aEnglish
000136438 082__ $$a540
000136438 1001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b0$$eFirst author
000136438 245__ $$aThe α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b).
000136438 260__ $$aBethesda, Md.$$bSoc.60645$$c2012
000136438 264_1 $$2Crossref$$3online$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2011-12-22
000136438 264_1 $$2Crossref$$3print$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2012-02-10
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000136438 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1586955128_28578
000136438 3367_ $$2BibTeX$$aARTICLE
000136438 3367_ $$2ORCID$$aJOURNAL_ARTICLE
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000136438 520__ $$aRegulated intramembrane proteolysis is a widely accepted concept describing the processing of various transmembrane proteins via ectodomain shedding followed by an intramembrane cleavage. The resulting cleavage products can be involved in reverse signaling. Presenilins, which constitute the active center of the γ-secretase complex, signal peptide peptidase (SPP), and its homologues, the SPP-like (SPPL) proteases are members of the family of intramembrane-cleaving aspartyl proteases of the GXGD-type. We recently demonstrated that Bri2 (itm2b) is a substrate for regulated intramembrane proteolysis by SPPL2a and SPPL2b. Intramembrane cleavage of Bri2 is triggered by an initial shedding event catalyzed by A Disintegrin and Metalloprotease 10 (ADAM10). Additionally primary sequence determinants within the intracellular domain, the transmembrane domain and the luminal juxtamembrane domain are required for efficient cleavage of Bri2 by SPPL2b. Using mutagenesis and circular dichroism spectroscopy we now demonstrate that a high α-helical content of the Bri2 transmembrane domain (TMD) reduces cleavage efficiency of Bri2 by SPPL2b, while the presence of a GXXXG dimerization motif influences the intramembrane cleavage only to a minor extent. Surprisingly, only one of the four conserved intramembrane glycine residues significantly affects the secondary structure of the Bri2 TMD and thereby its intramembrane cleavage. Other glycine residues do not influence the α-helical content of the transmembrane domain nor its intramembrane processing.
000136438 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000136438 588__ $$aDataset connected to CrossRef, PubMed,
000136438 650_7 $$2NLM Chemicals$$aITM2B protein, human
000136438 650_7 $$2NLM Chemicals$$aMembrane Glycoproteins
000136438 650_7 $$2NLM Chemicals$$aMembrane Proteins
000136438 650_7 $$0EC 3.4.-$$2NLM Chemicals$$aAmyloid Precursor Protein Secretases
000136438 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aAspartic Acid Endopeptidases
000136438 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aSPPL2b protein, human
000136438 650_7 $$0EC 3.4.24.-$$2NLM Chemicals$$aADAM Proteins
000136438 650_7 $$0EC 3.4.24.81$$2NLM Chemicals$$aADAM10 Protein
000136438 650_7 $$0EC 3.4.24.81$$2NLM Chemicals$$aADAM10 protein, human
000136438 650_2 $$2MeSH$$aADAM Proteins: genetics
000136438 650_2 $$2MeSH$$aADAM Proteins: metabolism
000136438 650_2 $$2MeSH$$aADAM10 Protein
000136438 650_2 $$2MeSH$$aAmino Acid Motifs
000136438 650_2 $$2MeSH$$aAmyloid Precursor Protein Secretases: genetics
000136438 650_2 $$2MeSH$$aAmyloid Precursor Protein Secretases: metabolism
000136438 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: genetics
000136438 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: metabolism
000136438 650_2 $$2MeSH$$aCircular Dichroism: methods
000136438 650_2 $$2MeSH$$aHEK293 Cells
000136438 650_2 $$2MeSH$$aHumans
000136438 650_2 $$2MeSH$$aMembrane Glycoproteins
000136438 650_2 $$2MeSH$$aMembrane Proteins: genetics
000136438 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000136438 650_2 $$2MeSH$$aMutagenesis
000136438 650_2 $$2MeSH$$aProtein Structure, Tertiary
000136438 650_2 $$2MeSH$$aProteolysis
000136438 7001_ $$0P:(DE-HGF)0$$aMartin, Lucas$$b1
000136438 7001_ $$0P:(DE-HGF)0$$aKlier, Bärbel$$b2
000136438 7001_ $$0P:(DE-HGF)0$$aHaug-Kröper, Martina$$b3
000136438 7001_ $$0P:(DE-HGF)0$$aGrammer, Gudula$$b4
000136438 7001_ $$0P:(DE-HGF)0$$aNuscher, Brigitte$$b5
000136438 7001_ $$0P:(DE-2719)2202037$$aHaass, Christian$$b6$$eLast author
000136438 77318 $$2Crossref$$3journal-article$$a10.1074/jbc.m111.328104$$b : American Society for Biochemistry & Molecular Biology (ASBMB), 2011-12-22$$n7$$p5156-5163$$tJournal of Biological Chemistry$$v287$$x0021-9258$$y2011
000136438 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M111.328104$$gVol. 287, no. 7, p. 5156 - 5163$$n7$$p5156-5163$$q287:7<5156 - 5163$$tThe journal of biological chemistry$$v287$$x0021-9258$$y2011
000136438 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3281599
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000136438 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2000007$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b0$$kDZNE
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000136438 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
000136438 9141_ $$y2012
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000136438 9201_ $$0I:(DE-2719)1110000-2$$kAG Fluhrer$$lSignal Peptide Peptidases as Models for γ-Secretase$$x0
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