| N-terminome analyses underscore the prevalence of SPPL3-mediated intramembrane proteolysis among Golgi-resident enzymes and its role in Golgi enzyme secretion. | N-terminome analyses underscore the prevalence of SPPL3-mediated intramembrane proteolysis among Golgi-resident enzymes and its role in Golgi enzyme secretion.
Hobohm L, Koudelka T, Bahr FH, Truberg J, Kapell S, Schacht SS, Meisinger D, Mengel M, Jochimsen A, Hofmann A, Heintz L, Tholey A, Voss M., Free PMC Article | 03/26/2022 |
| SPPL3-dependent downregulation of the synthesis of (neo)lacto-series glycosphingolipid is required for the staining of cell surface CD59. | SPPL3-dependent downregulation of the synthesis of (neo)lacto-series glycosphingolipid is required for the staining of cell surface CD59.
Kawaguchi K, Yamamoto-Hino M, Goto S. | 11/22/2021 |
| The SPPL3-Defined Glycosphingolipid Repertoire Orchestrates HLA Class I-Mediated Immune Responses. | The SPPL3-Defined Glycosphingolipid Repertoire Orchestrates HLA Class I-Mediated Immune Responses.
Jongsma MLM, de Waard AA, Raaben M, Zhang T, Cabukusta B, Platzer R, Blomen VA, Xagara A, Verkerk T, Bliss S, Kong X, Gerke C, Janssen L, Stickel E, Holst S, Plomp R, Mulder A, Ferrone S, Claas FHJ, Heemskerk MHM, Griffioen M, Halenius A, Overkleeft H, Huppa JB, Wuhrer M, Brummelkamp TR, Neefjes J, Spaapen RM., Free PMC Article | 09/11/2021 |
| Data suggest that activation of the metalloproteinase ADAM10 by signal peptide peptidase-like 3 (SPPL3) triggered by mutant BRAF(V600E) was a critical transformation event. | Multiepitope tissue analysis reveals SPPL3-mediated ADAM10 activation as a key step in the transformation of melanocytes.
Ostalecki C, Lee JH, Dindorf J, Collenburg L, Schierer S, Simon B, Schliep S, Kremmer E, Schuler G, Baur AS. | 12/2/2017 |
| Secretome analysis identifies novel signal Peptide peptidase-like 3 substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways | Secretome analysis identifies novel signal Peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways.
Kuhn PH, Voss M, Haug-Kröper M, Schröder B, Schepers U, Bräse S, Haass C, Lichtenthaler SF, Fluhrer R, Kuhn PH, Voss M, Haug-Kröper M, Schröder B, Schepers U, Bräse S, Haass C, Lichtenthaler SF, Fluhrer R., Free PMC Articles: PMC4458722, PMC4458722 | 03/5/2016 |
| Authors demonstrate that SPPL3 alters the pattern of cellular N-glycosylation by triggering the proteolytic release of active site-containing ectodomains of glycosidases and glycosyltransferases. | Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation.
Voss M, Künzel U, Higel F, Kuhn PH, Colombo A, Fukumori A, Haug-Kröper M, Klier B, Grammer G, Seidl A, Schröder B, Obst R, Steiner H, Lichtenthaler SF, Haass C, Fluhrer R, Voss M, Künzel U, Higel F, Kuhn PH, Colombo A, Fukumori A, Haug-Kröper M, Klier B, Grammer G, Seidl A, Schröder B, Obst R, Steiner H, Lichtenthaler SF, Haass C, Fluhrer R., Free PMC Articles: PMC4282638, PMC4282638 | 07/25/2015 |
| SPPL3 substrates identified on a proteome-wide scale in human and murine cells include numerous glycan-modifying enzymes residing in the Golgi network and implicated in distinct glycosylation pathways, including N-glycosylation, mucin-type O-glycosylation, O-mannosylation and glycosaminoglycan biosynthesis. | Secretome analysis identifies novel signal Peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways.
Kuhn PH, Voss M, Haug-Kröper M, Schröder B, Schepers U, Bräse S, Haass C, Lichtenthaler SF, Fluhrer R, Kuhn PH, Voss M, Haug-Kröper M, Schröder B, Schepers U, Bräse S, Haass C, Lichtenthaler SF, Fluhrer R., Free PMC Articles: PMC4458722, PMC4458722 | 04/8/2015 |
| SPPL3 cleaves Golgi type II membrane proteins leading to their secretion. SPPL3 substrates include Golgi glycosyltransferases MGAT5, B4GALT1, and B3GNT1. By facilitating disengagement of these glycosyltransferases from their membrane anchors, SPPL3 causes their premature secretion and consequently orchestrates the extent of N-glycosylation on human and murine cells. | Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation.
Voss M, Künzel U, Higel F, Kuhn PH, Colombo A, Fukumori A, Haug-Kröper M, Klier B, Grammer G, Seidl A, Schröder B, Obst R, Steiner H, Lichtenthaler SF, Haass C, Fluhrer R, Voss M, Künzel U, Higel F, Kuhn PH, Colombo A, Fukumori A, Haug-Kröper M, Klier B, Grammer G, Seidl A, Schröder B, Obst R, Steiner H, Lichtenthaler SF, Haass C, Fluhrer R., Free PMC Articles: PMC4282638, PMC4282638 | 04/8/2015 |
| SPPL3 enhances the signal-induced association of stromal interaction molecule 1 | A protease-independent function for SPPL3 in NFAT activation.
Makowski SL, Wang Z, Pomerantz JL., Free PMC Article | 03/21/2015 |
| human SPPL3 is the first GxGD-type aspartyl protease shown to be capable of acting like a sheddase, similar to members of the rhomboid family, which belong to the class of intramembrane-cleaving serine proteases. | Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3).
Voss M, Fukumori A, Kuhn PH, Künzel U, Klier B, Grammer G, Haug-Kröper M, Kremmer E, Lichtenthaler SF, Steiner H, Schröder B, Haass C, Fluhrer R., Free PMC Article | 03/2/2013 |
| SPPL2b is targeted through the secretory pathway to endosomes/lysosomes, whereas SPP and SPPL3 are restricted to the ER. | Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3.
Krawitz P, Haffner C, Fluhrer R, Steiner H, Schmid B, Haass C. | 01/21/2010 |
| SPPL3 cleaves a SPP substrate, but a more distantly related homologue SPPL2b does not, providing strong evidence that the malaria SPP and human SPPL3 have conserved active sites, while the active sites SPPL2b is distinct | Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase.
Nyborg AC, Ladd TB, Jansen K, Kukar T, Golde TE. | 01/21/2010 |
| SPP, SPPL2a, -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis | Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins.
Friedmann E, Lemberg MK, Weihofen A, Dev KK, Dengler U, Rovelli G, Martoglio B. | 01/21/2010 |