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000140604 0247_ $$2doi$$a10.15252/embr.201846449
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000140604 0247_ $$2ISSN$$a1469-221X
000140604 0247_ $$2ISSN$$a1469-3178
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000140604 037__ $$aDZNE-2020-06926
000140604 041__ $$aEnglish
000140604 082__ $$a570
000140604 1001_ $$0P:(DE-HGF)0$$aNiemeyer, Johannes$$b0
000140604 245__ $$aThe intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban.
000140604 260__ $$aHoboken, NJ [u.a.]$$bWiley$$c2019
000140604 264_1 $$2Crossref$$3online$$bEMBO$$c2019-02-07
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000140604 520__ $$aSignal peptide peptidase (SPP) and the four homologous SPP-like (SPPL) proteases constitute a family of intramembrane aspartyl proteases with selectivity for type II-oriented transmembrane segments. Here, we analyse the physiological function of the orphan protease SPPL2c, previously considered to represent a non-expressed pseudogene. We demonstrate proteolytic activity of SPPL2c towards selected tail-anchored proteins. Despite shared ER localisation, SPPL2c and SPP exhibit distinct, though partially overlapping substrate spectra and inhibitory profiles, and are organised in different high molecular weight complexes. Interestingly, SPPL2c is specifically expressed in murine and human testis where it is primarily localised in spermatids. In mice, SPPL2c deficiency leads to a partial loss of elongated spermatids and reduced motility of mature spermatozoa, but preserved fertility. However, matings of male and female SPPL2c-/- mice exhibit reduced litter sizes. Using proteomics we identify the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2)-regulating protein phospholamban (PLN) as a physiological SPPL2c substrate. Accumulation of PLN correlates with a decrease in intracellular Ca2+ levels in elongated spermatids that likely contribute to the compromised male germ cell differentiation and function of SPPL2c-/- mice.
000140604 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000140604 542__ $$2Crossref$$i2019-02-07$$uhttp://onlinelibrary.wiley.com/termsAndConditions#vor
000140604 542__ $$2Crossref$$i2019-02-07$$uhttp://doi.wiley.com/10.1002/tdm_license_1.1
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000140604 650_2 $$2MeSH$$aAmino Acid Sequence
000140604 650_2 $$2MeSH$$aAnimals
000140604 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: chemistry
000140604 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: metabolism
000140604 650_2 $$2MeSH$$aCalcium: metabolism
000140604 650_2 $$2MeSH$$aCalcium-Binding Proteins: metabolism
000140604 650_2 $$2MeSH$$aCell Membrane: enzymology
000140604 650_2 $$2MeSH$$aEndoplasmic Reticulum: metabolism
000140604 650_2 $$2MeSH$$aFemale
000140604 650_2 $$2MeSH$$aGerm Cells: metabolism
000140604 650_2 $$2MeSH$$aHEK293 Cells
000140604 650_2 $$2MeSH$$aHeLa Cells
000140604 650_2 $$2MeSH$$aHomeostasis
000140604 650_2 $$2MeSH$$aHumans
000140604 650_2 $$2MeSH$$aMale
000140604 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000140604 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000140604 650_2 $$2MeSH$$aMice
000140604 650_2 $$2MeSH$$aOrgan Specificity
000140604 650_2 $$2MeSH$$aSpermatids: metabolism
000140604 650_2 $$2MeSH$$aSubstrate Specificity
000140604 650_2 $$2MeSH$$aTestis: enzymology
000140604 7001_ $$0P:(DE-HGF)0$$aMentrup, Torben$$b1
000140604 7001_ $$0P:(DE-HGF)0$$aHeidasch, Ronny$$b2
000140604 7001_ $$0P:(DE-2719)2810938$$aMüller, Stephan A$$b3$$udzne
000140604 7001_ $$0P:(DE-HGF)0$$aBiswas, Uddipta$$b4
000140604 7001_ $$0P:(DE-HGF)0$$aMeyer, Rieke$$b5
000140604 7001_ $$0P:(DE-HGF)0$$aPapadopoulou, Alkmini A$$b6
000140604 7001_ $$aDederer, Verena$$b7
000140604 7001_ $$aHaug-Kröper, Martina$$b8
000140604 7001_ $$aAdamski, Vivian$$b9
000140604 7001_ $$aLüllmann-Rauch, Renate$$b10
000140604 7001_ $$aBergmann, Martin$$b11
000140604 7001_ $$aMayerhofer, Artur$$b12
000140604 7001_ $$aSaftig, Paul$$b13
000140604 7001_ $$aWennemuth, Gunther$$b14
000140604 7001_ $$aJessberger, Rolf$$b15
000140604 7001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b16$$udzne
000140604 7001_ $$0P:(DE-2719)2181459$$aLichtenthaler, Stefan F$$b17$$udzne
000140604 7001_ $$aLemberg, Marius K$$b18
000140604 7001_ $$0P:(DE-HGF)0$$aSchröder, Bernd$$b19$$eCorresponding author
000140604 77318 $$2Crossref$$3journal-article$$a10.15252/embr.201846449$$b : EMBO, 2019-02-07$$n3$$tEMBO reports$$v20$$x1469-221X$$y2019
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000140604 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC6399600
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000140604 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2810938$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b3$$kDZNE
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000140604 9131_ $$0G:(DE-HGF)POF3-342$$1G:(DE-HGF)POF3-340$$2G:(DE-HGF)POF3-300$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bGesundheit$$lErkrankungen des Nervensystems$$vDisease Mechanisms and Model Systems$$x0
000140604 9141_ $$y2019
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000140604 9201_ $$0I:(DE-2719)1110007$$kAG Haass$$lMolecular Neurodegeneration$$x0
000140604 9201_ $$0I:(DE-2719)1110000-2$$kAG Fluhrer$$lSignal Peptide Peptidases as Models for γ-Secretase$$x1
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