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000140605 0247_ $$2ISSN$$a1469-221X
000140605 0247_ $$2ISSN$$a1469-3178
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000140605 037__ $$aDZNE-2020-06927
000140605 041__ $$aEnglish
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000140605 1001_ $$0P:(DE-HGF)0$$aPapadopoulou, Alkmini A$$b0
000140605 245__ $$aSignal Peptide Peptidase-Like 2c (SPPL2c) impairs vesicular transport and cleaves SNARE proteins.
000140605 260__ $$aHoboken, NJ [u.a.]$$bWiley$$c2019
000140605 264_1 $$2Crossref$$3online$$bEMBO$$c2019-02-07
000140605 264_1 $$2Crossref$$3print$$bEMBO$$c2019-03-01
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000140605 500__ $$aTitle corrected according to Corrigendum: EMBO rep (2019) 20: e48133 https://doi.org/10.15252/embr.201948133
000140605 520__ $$aMembers of the GxGD-type intramembrane aspartyl proteases have emerged as key players not only in fundamental cellular processes such as B-cell development or protein glycosylation, but also in development of pathologies, such as Alzheimer's disease or hepatitis virus infections. However, one member of this protease family, signal peptide peptidase-like 2c (SPPL2c), remains orphan and its capability of proteolysis as well as its physiological function is still enigmatic. Here, we demonstrate that SPPL2c is catalytically active and identify a variety of SPPL2c candidate substrates using proteomics. The majority of the SPPL2c candidate substrates cluster to the biological process of vesicular trafficking. Analysis of selected SNARE proteins reveals proteolytic processing by SPPL2c that impairs vesicular transport and causes retention of cargo proteins in the endoplasmic reticulum. As a consequence, the integrity of subcellular compartments, in particular the Golgi, is disturbed. Together with a strikingly high physiological SPPL2c expression in testis, our data suggest involvement of SPPL2c in acrosome formation during spermatogenesis.
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000140605 542__ $$2Crossref$$i2019-02-07$$uhttp://doi.wiley.com/10.1002/tdm_license_1.1
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000140605 7001_ $$0P:(DE-2719)2810938$$aMüller, Stephan A$$b1$$udzne
000140605 7001_ $$0P:(DE-HGF)0$$aMentrup, Torben$$b2
000140605 7001_ $$0P:(DE-2719)2812458$$aShmueli, Merav D$$b3$$udzne
000140605 7001_ $$0P:(DE-HGF)0$$aNiemeyer, Johannes$$b4
000140605 7001_ $$0P:(DE-HGF)0$$aHaug-Kröper, Martina$$b5
000140605 7001_ $$0P:(DE-HGF)0$$avon Blume, Julia$$b6
000140605 7001_ $$0P:(DE-HGF)0$$aMayerhofer, Artur$$b7
000140605 7001_ $$0P:(DE-2719)2812867$$aFeederle, Regina$$b8$$udzne
000140605 7001_ $$0P:(DE-HGF)0$$aSchröder, Bernd$$b9
000140605 7001_ $$0P:(DE-2719)2181459$$aLichtenthaler, Stefan F$$b10$$udzne
000140605 7001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b11$$eLast author$$udzne
000140605 77318 $$2Crossref$$3journal-article$$a10.15252/embr.201846451$$b : EMBO, 2019-02-07$$n3$$tEMBO reports$$v20$$x1469-221X$$y2019
000140605 773__ $$0PERI:(DE-600)2025376-X$$a10.15252/embr.201846451$$gVol. 20, no. 3$$n3$$pe46451$$q20:3$$tEMBO reports$$v20$$x1469-221X$$y2019
000140605 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC6399617
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000140605 9141_ $$y2019
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000140605 9201_ $$0I:(DE-2719)1110007$$kAG Haass$$lMolecular Neurodegeneration$$x0
000140605 9201_ $$0I:(DE-2719)1110006$$kAG Lichtenthaler$$lNeuroproteomics$$x1
000140605 9201_ $$0I:(DE-2719)1140004$$kAG Feederle$$lAntibody Production$$x2
000140605 9201_ $$0I:(DE-2719)1110000-2$$kAG Fluhrer$$lSignal Peptide Peptidases as Models for γ-Secretase$$x3
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