Publikationen

  • Niemeyer,J., Mentrup,T., Heidasch,R., Müller,S.A., Biswas,U., Meyer,R., Papadopoulou,A., Dederer,V., Haug-Kröper,M., Adamski,V., Lüllmann-Rauch,R., Bergmann,M., Mayerhofer,A., Saftig,P., Wennemuth,G., Jessberger,R., Fluhrer,R., Lichtenthaler, S.F., Lemberg,M., and Schröder,B. (2019)
    The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban. EMBO Rep 20, e46449.

  • Papadopoulou,A., Müller,S.A., Mentrup,T., Shmueli,M.D., Niemeyer,J., Haug-Kröper,M., von Blume,J., Mayerhofer,A., Feederle,R., Schröder,B., Lichtenthaler,S.F. and Fluhrer,R. (2019)
    Signal Peptide-Peptidase-Like 2c (SPPL2c impairs vesicular transport by cleavage of SNARE proteins. EMBO Rep 20, e46451.

  • Mentrup,T., Theodorou,K., Cabrera-Cabrera,F., Helbig,A.O., Happ,K., Gijbels, M., Gradtke, A.C., Rabe,B., Fukumori, A., Steiner, H., Tholey,A., Fluhrer,R., Donners,M. and Schröder,B. (2019)
    Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis. J Exp Med 216, 807-830.
  • Kong,X.F., Martinez-Barricarte,R., Kennedy, J., Mele,F., Lazarov,T., Deenick,E.K., Ma,C.S., Breton,G., Lucero, K.B., Langlais,D., Bousfiha,A., Aytekin,C., Markle,J., Trouillet,C., Jabot-Hanin,F., Arlehamn,C.S.L., Rao,G., Picard,C., Lasseau,T., Latorre,D., Hambleton,S., Deswarte,C., Itan,Y., Abarca,K., Moraes-Vasconcelos,D., Ailal,F., Ikinciogullari,A., Dogu,F., Benhsaien,I., Sette,A., Abel,L., Boisson-Dupuis,S., Schröder,B., Nussenzweig,M.C., Liu,K., Geissmann,F., Tangye,S.G., Gros,P., Sallusto,F., Bustamante,J., Casanova, J.L. (2018)
    Disruption of an antimycobacterial circuit between dendritic and helper T cells in human SPPL2a deficiency. Nat Immunol., 19, 973-985.
  • Dudeck,J., Medyukhina,A., Fröbel,J., Svensson,C.M., Kotrba,J., Gerlach,M., Gradtke,A.C., Schröder,B., Speier,S., Figge,M.T., Dudeck,A. (2017)
    Mast cells acquire MHCII from dendritic cells during skin inflammation. J. Exp. Med., 214, 3791-38
  • Mentrup,T., Loock,A.C., Fluhrer,R. and Schröder,B. (2017)
    Signal peptide peptidase and SPP-like proteases - possible therapeutic targets? Biochim. Biophys. Acta, 1864, 2169-2182.
  • Schneppenheim,J., Loock,A.C., Hüttl,S., Schweizer,M., Lüllmann-Rauch,R., Oberg,H.H., Arnold,P., Lehmann,C., Dudziak,D., Kabelitz,D., Lucius,R., Lennon-Duménil,A.M., Saftig,P., and Schröder,B. (2017)
    The influence of MHC class II on B cell defects induced by Invariant chain/CD74 N-terminal fragments.     J. Immunol., 199, 172-185.
  • Nguyen,T.L., Schneppenheim,J., Rudnik,S., Lüllmann-Rauch,R., Bernreuther,C., Hermans-Borgmeyer,I., Glatzel,M., Saftig,P. and Schröder,B. (2017)
    Functional characterization of the lysosomal membrane protein TMEM192 in mice. Oncotarget, 8, 43635-43652.
  • Mentrup,T., Fluhrer, R. and Schröder,B. (2017)
    Latest emerging functions of SPP/SPPL intramembrane proteases. Eur J Cell Biol, 96, 372-382.         
  • Schröder,B. and Saftig,P. (2016)
    Intramembrane proteolysis within lysosomes. Ageing Res Rev, 32, 51-64.           
  • Schröder,B. (2016)
    The multifaceted roles of the invariant chain CD74 - More than just a chaperone.     Biochim. Biophys. Acta, 1863, 1269-1281                                              
  • Hüttl,S., Helfrich,F., Mentrup,T., Held,S., Fukumori,A., Steiner,H., Saftig,P., Fluhrer,R., and Schröder,B. (2016)
    Substrate determinants of Signal peptide peptidase-like 2a (SPPL2a)-mediated Intramembrane Proteolysis of the Invariant chain CD74.     Biochem. J., 473, 1405-1422.
  • Klionsky,D.J., Abdelmohsen,K.,…, Schröder,B.,…, Zughaier, S.M. (2016)
    Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition), Autophagy, 12, 1-222.
  • Hüttl,S., Kläsener,K., Schweizer,M., Schneppenheim,J., Oberg,H.H., Kabelitz,D., Reth,M., Saftig,P., and Schröder,B. (2015)
    Processing of CD74 by the intramembrane protease SPPL2a is critical for B cell receptor signaling in transitional B cells J. Immunol., 195, 1548-1563.                    
  • Mentrup,T., Häsler,R., Fluhrer,R., Saftig,P., and Schröder,B. (2015)
    A cell-based assay reveals nuclear translocation of intracellular domains released by SPPL proteases. Traffic, 16, 871-892.      
  • Kuhn,P.H., Voss,M., Haug-Kröper,M., Schröder,B., Schepers,U., Bräse,S., Haass,C., Lichtenthaler,S.F., and Fluhrer,R. (2015)
    Secretome analysis identifies novel signal peptide peptidase-like 3 (SPPL3) substrates and reveals a role of SPPL3 in multiple Golgi glycosylation pathways. Mol Cell Prot, 14, 1584-1598.
  • Voss,M., Künzel,U., Higel,F., Kuhn,P.H., Colombo,A., Fukumori,A., Haug-Kröper,M., Klier,B., Grammer,G., Seidl,A., Schröder,B., Obst,R., Steiner,H., Lichtenthaler,S.F., Haass,C., and Fluhrer,R. (2014)
    Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation. EMBO J, 33, 2809-2905.  
  • Grimm,C., Holdt,L.M., Chen,C.C., Hassan,S., Müller, C., Jörs, S., Cuny,H., Kissing S., Schröder,B., Butz,E., Northoff,B., Castonguay, J., Luber,C.A., Moser,M., Spahn,S., Lüllman-Rauch,R., Fendel,C., Klugbauer,N., Griesbeck,O., Haas,A., Mann,M., Bracher,F., Teupser,D., Saftig,P., Biel,M. and Wahl-Schott,C. (2014)
    High susceptibility to fatter liver disease in two-pore channel 2-deficient mice. Nat Commun, 5, 4699.                               
  • Schneppenheim,J., Hüttl,S. Kruchen,A., Fluhrer,R. Müller,I., Saftig,P., Schneppenheim,R., Martin,C.L. and Schröder,B. (2014)
    Signal-peptide-peptidase-like 2a is required for CD74 intramembrane proteolysis in human B cells. Biochem Biophys Res Commun, 451, 48-53.
  • Videm,P., Gunasekaran,D., Schröder,B., Mayer,B., Biniossek,M.L. and Schilling,O. (2014)
    Automated Peptide Mapping and Protein-Topographical Annotation of Proteomics Data. BMC Bioinformatics, 15, 207.                     
  • Schneppenheim,J., Hüttl,S., Mentrup,T, Lüllmann-Rauch,R., Rothaug,M., Engelke,M., Dittmann,K., Dressel,R., Araki,M., Araki,K., Wienands,J., Fluhrer,R., Saftig,P. and Schröder,B. (2014)
    The intramembrane proteases Signal-peptide-peptidase-like 2a/b have distinct functions in vivo. Mol Cell Biol, 34, 1398-1411.
  • Kraft,S., Jouvin,M.H., Kulkarni, N., Kissing,S., Morgan,E.S., Dvorak,A.M., Schröder,B., Saftig,P. and Kinet,J.P. (2013)
    The tetraspanin CD63 is required for efficient IgE-mediated mast cell degranulation and anaphylaxis. J. Immunol., 191, 2871-2878.
  • Voss,M., Schröder,B. and Fluhrer,R.(2013)
    Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases. Biochim. Biophys. Acta, 1828, 2828-2839.            
  • Bronckers,A., Güneli,N., Lüllmann-Rauch,R., Schneppenheim,J., Moraru,A.P., Himmerkus,N., Bervoets,T.J., Fluhrer, R., Everts,V., Saftig,P. and Schröder,B. (2013) The intramembrane protease SPPL2A is critical for tooth enamel formation. J Bone Miner Res, 28, 1622-1630.             
  • Schwake,M., Schröder,B. and Saftig,P. (2013)
    Lysosomal Membrane Proteins and their central role in physiology. Traffic, 14, 739-748.                         
  • Schneppenheim,J., Dressel,R., Hüttl,S.,Lüllmann-Rauch,R., Engelke,M., Dittmann,K., Wienands,J., Eskelinen,E.L., Hermans-Borgmeyer,I., Fluhrer,R., Saftig,P., and Schröder,B. (2013)
    The intramembrane protease SPPL2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain. J. Exp. Med., 210, 41-58.
  • Voss,M., Fukumori,A., Kuhn, P.H., Künzel, U., Klier,B., Grammer,G., Haug-Kröper,M., Kremmer,E., Lichtenthaler,S., Steiner,H., Schröder,B., Haass,C., and Fluhrer,R. (2012)
    Foamy virus envelope protein is a substrate for signal peptide peptidase like-3 (SPPL3). J. Biol. Chem., 287 (52), 43401-43409.                  
  • Behnke,J., Schneppenheim,J., Koch-Nolte,F., Haag,F., Saftig,P., and Schröder,B. (2011)
    Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endsosomes by a tyrosine motif in ist C-terminal tail. FEBS Lett, 585, 2951-2957.
  • Savalas,L.R.T., Gasnier,B., Damme,M., Lübke,T., Wrocklage,C., Debacker,C., Jézégou,A., Reinheckel,T., Hasilik,A., Saftig,P., and Schröder,B. (2011).
    “Disrupted in renal carcinoma 2” (DIRC2) - a novel transporter of the lysosomal membrane - is proteolytically processed by cathepsin L. Biochem. J., 439, 113-128.
  • Behnke, J., Eskelinen,E.L:, Saftig,P., and Schröder,B. (2011).
    Two dileucine motifs mediate late endosomal/lysosomal targeting of Transmembrane protein 192 (TMEM192) and a C-terminal cysteine residue is responsible for disulfide bond formation in TMEM192 homodimers. Biochem .J. 434, 219-231.
  • Saftig,P., Schröder,B., and Blanz,J. (2010).
    Lysosomal membrane proteins: life between acid and neutral conditions. Biochem. Soc. Trans. 38, 1420-1423.                   
  • Schröder,B., Wrocklage,C., Hasilik,A., and Saftig,P. (2010).
    The proteome of lysosomes. Proteomics 10, 4053-4076. 
  • Schröder,B. and  Saftig,P. (2010).
    Molecular insights into mechanisms of intramembrane proteolysis by signal peptide peptidase (SPP). Biochem. J. 427, 1-3.                    
  • Schröder,B., Wrocklage,C., Hasilik,A., and Saftig,P. (2010).
    Molecular characterisation of 'transmembrane protein 192' (TMEM192), a novel protein of the lysosomal membrane. Biol Chem. 391, 695-704.                                 
  • Hasilik,A., Wrocklage,C., and Schröder,B. (2009).
    Intracellular trafficking of lysosomal proteins and lysosomes. Int. J. Clin. Pharmacol. Ther. 47 (Suppl.1), S18-33.                                    
  • Schieweck,O., Damme,M., Schröder,B., Hasilik,A., Schmidt,B., and Lübke,T. (2009). NCU-G1 is a highly glycosylated integral membrane protein of the lysosome. Biochem. J. 422, 83-90.                                                                             
  • Schröder,J., Lüllmann-Rauch,R., Himmerkus,N., Pleines,I., Nieswandt,B., Orinska,Z., Koch-Nolte,F., Schröder,B., Bleich,M., and Saftig,P. (2009).
    Deficiency of the tetraspanin CD63 associated with kidney pathology but normal lysosomal function. Mol.Cell Biol. 29, 1083-1094. 
  • Beertsen,W., Willenborg,M., Everts,V., Zirogianni,A., Podschun,R., Schröder,B., Eskelinen,E.L., and Saftig,P. (2008).
    Impaired phagosomal maturation in neutrophils leads to periodontitis in lysosomal-associated membrane protein-2 knockout mice.J. Immunol. 180, 475-482.             
  • Schröder,B., Wrocklage,C., Pan,C., Jäger,R., Kösters,B., Schäfer,H., Elsässer,H.P., Mann,M., and Hasilik,A. (2007).
    Integral and Associated Lysosomal Membrane Proteins. Traffic 8, 1676-1686.   
  • Schröder,B., Elsässer,H.P., Schmidt,B., and Hasilik,A. (2007).
    Characterisation of lipofuscin-like lysosomal inclusion bodies from human placenta. FEBS Lett. 581, 102-108.                                      
  • Schröder,B. and Hasilik,A. (2006).
    A protocol for combined delipidation and subfractionation of membrane proteins using organic solvents. Anal. Biochem. 357, 144-146.                              
  • Melcher,R., Hillebrand,A., Bahr,U., Schröder,B., Karas,M., and Hasilik,A. (2000). Glycosylation-site-selective synthesis of N-acetyl-lactosamine repeats in bis-glycosylated human lysozyme. Biochem. J. 348, 507-515.

Zu dieser Seite

Andrea Heinze
Letzte Änderung: 18.07.2019