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000151555 0247_ $$2pmid$$apmid:32052089
000151555 0247_ $$2doi$$a10.1007/s00018-020-03470-6
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000151555 037__ $$aDZNE-2020-01139
000151555 041__ $$aEnglish
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000151555 1001_ $$aMentrup, Torben$$b0
000151555 245__ $$aPhysiological functions of SPP/SPPL intramembrane proteases
000151555 260__ $$aCham (ZG)$$bSpringer International Publishing AG$$c2020
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000151555 520__ $$aIntramembrane proteolysis describes the cleavage of substrate proteins within their hydrophobic transmembrane segments. Several families of intramembrane proteases have been identified including the aspartyl proteases Signal peptide peptidase (SPP) and its homologues, the SPP-like (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and SPPL3. As presenilin homologues, they employ a similar catalytic mechanism as the well-studied γ-secretase. However, SPP/SPPL proteases cleave transmembrane proteins with a type II topology. The characterisation of SPP/SPPL-deficient mouse models has highlighted a still growing spectrum of biological functions and also promoted the substrate discovery of these proteases. In this review, we will summarise the current hypotheses how phenotypes of these mouse models are linked to the molecular function of the enzymes. At the cellular level, SPP/SPPL-mediated cleavage events rather provide specific regulatory switches than unspecific bulk proteolysis. By this means, a plethora of different cell biological pathways is influenced including signal transduction, membrane trafficking and protein glycosylation.
000151555 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000151555 542__ $$2Crossref$$i2020-02-12$$uhttps://creativecommons.org/licenses/by/4.0
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000151555 650_2 $$2MeSH$$aAmyloid Precursor Protein Secretases: metabolism
000151555 650_2 $$2MeSH$$aAnimals
000151555 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: chemistry
000151555 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: metabolism
000151555 650_2 $$2MeSH$$aHumans
000151555 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000151555 650_2 $$2MeSH$$aProtein Transport
000151555 650_2 $$2MeSH$$aProteolysis
000151555 650_2 $$2MeSH$$aSignal Transduction
000151555 650_2 $$2MeSH$$aSubstrate Specificity
000151555 7001_ $$aCabrera-Cabrera, Florencia$$b1
000151555 7001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b2$$udzne
000151555 7001_ $$00000-0003-0774-6270$$aSchröder, Bernd$$b3$$eCorresponding author
000151555 77318 $$2Crossref$$3journal-article$$a10.1007/s00018-020-03470-6$$b : Springer Science and Business Media LLC, 2020-02-12$$n15$$p2959-2979$$tCellular and Molecular Life Sciences$$v77$$x1420-682X$$y2020
000151555 773__ $$0PERI:(DE-600)1458497-9$$a10.1007/s00018-020-03470-6$$gVol. 77, no. 15, p. 2959 - 2979$$n15$$p2959-2979$$tCellular and molecular life sciences$$v77$$x1420-682X$$y2020
000151555 8564_ $$uhttps://link.springer.com/article/10.1007/s00018-020-03470-6
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