Home > Publications Database > The α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b). > print

001     136438
005     20240321220052.0
024 7 _ |a 10.1074/jbc.M111.328104
|2 doi
024 7 _ |a pmid:22194595
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024 7 _ |a pmc:PMC3281599
|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-2020-02760
041 _ _ |a English
082 _ _ |a 540
100 1 _ |a Fluhrer, Regina
|0 P:(DE-2719)2000007
|b 0
|e First author
245 _ _ |a The α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b).
260 _ _ |a Bethesda, Md.
|c 2012
|b Soc.60645
264 _ 1 |3 online
|2 Crossref
|b American Society for Biochemistry & Molecular Biology (ASBMB)
|c 2011-12-22
264 _ 1 |3 print
|2 Crossref
|b American Society for Biochemistry & Molecular Biology (ASBMB)
|c 2012-02-10
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 1586955128_28578
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336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
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520 _ _ |a Regulated 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.
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 ITM2B protein, human
|2 NLM Chemicals
650 _ 7 |a Membrane Glycoproteins
|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 Aspartic Acid Endopeptidases
|0 EC 3.4.23.-
|2 NLM Chemicals
650 _ 7 |a SPPL2b protein, human
|0 EC 3.4.23.-
|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 ADAM Proteins: genetics
|2 MeSH
650 _ 2 |a ADAM Proteins: metabolism
|2 MeSH
650 _ 2 |a ADAM10 Protein
|2 MeSH
650 _ 2 |a Amino Acid Motifs
|2 MeSH
650 _ 2 |a Amyloid Precursor Protein Secretases: genetics
|2 MeSH
650 _ 2 |a Amyloid Precursor Protein Secretases: metabolism
|2 MeSH
650 _ 2 |a Aspartic Acid Endopeptidases: genetics
|2 MeSH
650 _ 2 |a Aspartic Acid Endopeptidases: metabolism
|2 MeSH
650 _ 2 |a Circular Dichroism: methods
|2 MeSH
650 _ 2 |a HEK293 Cells
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Membrane Glycoproteins
|2 MeSH
650 _ 2 |a Membrane Proteins: genetics
|2 MeSH
650 _ 2 |a Membrane Proteins: metabolism
|2 MeSH
650 _ 2 |a Mutagenesis
|2 MeSH
650 _ 2 |a Protein Structure, Tertiary
|2 MeSH
650 _ 2 |a Proteolysis
|2 MeSH
700 1 _ |a Martin, Lucas
|0 P:(DE-HGF)0
|b 1
700 1 _ |a Klier, Bärbel
|0 P:(DE-HGF)0
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700 1 _ |a Haug-Kröper, Martina
|0 P:(DE-HGF)0
|b 3
700 1 _ |a Grammer, Gudula
|0 P:(DE-HGF)0
|b 4
700 1 _ |a Nuscher, Brigitte
|0 P:(DE-HGF)0
|b 5
700 1 _ |a Haass, Christian
|0 P:(DE-2719)2202037
|b 6
|e Last author
773 1 8 |a 10.1074/jbc.m111.328104
|b : American Society for Biochemistry & Molecular Biology (ASBMB), 2011-12-22
|n 7
|p 5156-5163
|3 journal-article
|2 Crossref
|t Journal of Biological Chemistry
|v 287
|y 2011
|x 0021-9258
773 _ _ |a 10.1074/jbc.M111.328104
|g Vol. 287, no. 7, p. 5156 - 5163
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856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3281599
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910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
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913 1 _ |a DE-HGF
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