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000139528 0247_ $$2doi$$a10.1016/j.ejcb.2017.03.002
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000139528 0247_ $$2ISSN$$a1618-1298
000139528 037__ $$aDZNE-2020-05850
000139528 041__ $$aEnglish
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000139528 1001_ $$0P:(DE-HGF)0$$aMentrup, Torben$$b0
000139528 245__ $$aLatest emerging functions of SPP/SPPL intramembrane proteases.
000139528 260__ $$aAmsterdam$$bElsevier74814$$c2017
000139528 264_1 $$2Crossref$$3print$$bElsevier BV$$c2017-08-01
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000139528 520__ $$aSignal peptide peptidase (SPP) and the four related SPP-like (SPPL) proteases are homologues of the presenilins, which comprise the catalytic centre of the γ-secretase complex. SPP/SPPL proteases are GxGD-type aspartyl intramembrane proteases selective for substrates with a type II membrane topology. Subcellular localisations of SPP/SPPL proteases range from the early secretory pathway to the plasma membrane and the endocytic system. Similarly diverse are their functional roles at the cellular level covering the turnover of signal peptides and membrane proteins, a contribution to the ERAD pathway as well as the regulation of cellular protein glycosylation and certain signaling pathways. Much less well understood are the physiological functions of SPP/SPPL proteases in complex organisms. Whereas a major role of SPPL2a for homeostasis of B cells and dendritic cells has been documented in mice, in vivo functions of SPP and the other SPPLs remain largely elusive to date. SPP/SPPL proteases contribute to regulated intramembrane proteolysis (RIP), a sequential processing of single-spanning transmembrane proteins by an ectodomain sheddase and an intramembrane-cleaving protease (I-CLIP). However, recent studies reported the cleavage of tail-anchored and multi-pass membrane proteins by SPP as well as the capability of SPPL3 to accept substrates without a preceding ectodomain shedding. This revealed that the mechanistic properties within this family are more diverse than initially thought. With this review, we aim to provide an update on recent achievements in defining the function and (patho-) physiological relevance of SPP/SPPL proteases and to highlight open questions in the field.
000139528 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000139528 650_7 $$2NLM Chemicals$$aMembrane Proteins
000139528 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aAspartic Acid Endopeptidases
000139528 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$asignal peptide peptidase
000139528 650_2 $$2MeSH$$aAnimals
000139528 650_2 $$2MeSH$$aAspartic Acid Endopeptidases
000139528 650_2 $$2MeSH$$aHumans
000139528 650_2 $$2MeSH$$aMembrane Proteins
000139528 7001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b1$$udzne
000139528 7001_ $$0P:(DE-HGF)0$$aSchröder, Bernd$$b2$$eCorresponding author
000139528 77318 $$2Crossref$$3journal-article$$a10.1016/j.ejcb.2017.03.002$$b : Elsevier BV, 2017-08-01$$n5$$p372-382$$tEuropean Journal of Cell Biology$$v96$$x0171-9335$$y2017
000139528 773__ $$0PERI:(DE-600)391967-5$$a10.1016/j.ejcb.2017.03.002$$gVol. 96, no. 5, p. 372 - 382$$n5$$p372-382$$q96:5<372 - 382$$tEuropean journal of cell biology$$v96$$x0171-9335$$y2017
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