Schröder, Bernd

[["dc.bibliographiccitation.firstpage","113"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","128"],["dc.bibliographiccitation.volume","439"],["dc.contributor.author","Savalas, Lalu Rudyat Telly"],["dc.contributor.author","Gasnier, Bruno"],["dc.contributor.author","Damme, Markus"],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Wrocklage, Christian"],["dc.contributor.author","Debacker, Cecile"],["dc.contributor.author","Jezegou, Adrien"],["dc.contributor.author","Reinheckel, Thomas"],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Saftig, Paul"],["dc.contributor.author","Schroeder, Bernd"],["dc.date.accessioned","2018-11-07T08:51:12Z"],["dc.date.available","2018-11-07T08:51:12Z"],["dc.date.issued","2011"],["dc.description.abstract","DIRC2 (Disrupted in renal carcinoma 2) has been initially identified as a breakpoint-spanning gene in a chromosomal translocation putatively associated with the development of renal cancer. The DIRC2 protein belongs to the MFS (major facilitator superfamily) and has been previously detected by organellar proteomics as a tentative constituent of lysosomal membranes. In the present study, lysosomal residence of overexpressed as well as endogenous DIRC2 was shown by several approaches. DIRC2 is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment respectively. Proteolytic cleavage occurs in lysosomal compartments and critically depends on the activity of cathepsin L which was found to be indispensable for this process in murine embryonic fibroblasts. The cleavage site within DIRC2 was mapped between amino acid residues 214 and 261 using internal epitope tags, and is presumably located within the tentative fifth intralysosomal loop, assuming the typical MFS topology. Lysosomal targeting of DIRC2 was demonstrated to be mediated by a N-terminal dileucine motif. By disrupting this motif, DIRC2 can be redirected to the plasma membrane. Finally, in a whole-cell electrophysiological assay based on heterologous expression of the targeting mutant at the plasma membrane of Xenopus oocytes, the application of a complex metabolic mixture evokes an outward current associated with the surface expression of full-length DIRC2. Taken together, these data strongly support the idea that DIRC2 is an electrogenic lysosomal metabolite transporter which is subjected to and presumably modulated by limited proteolytic processing."],["dc.identifier.doi","10.1042/BJ20110166"],["dc.identifier.isi","000295767100011"],["dc.identifier.pmid","21692750"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21878"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.relation.issn","0264-6021"],["dc.title","Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","102"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","108"],["dc.bibliographiccitation.volume","581"],["dc.contributor.author","Schroeder, Bernd"],["dc.contributor.author","Elsaesser, Hans-Peter"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Hasilik, Andrej"],["dc.date.accessioned","2018-11-07T11:05:44Z"],["dc.date.available","2018-11-07T11:05:44Z"],["dc.date.issued","2007"],["dc.description.abstract","A structural hallmark of lysosomes is heterogeneity of their contents. We describe a method for isolation of particulate materials from human placental lysosomes. After a methionine methyl ester-induced disruption of lysosomes and two density gradient centrifugations we obtained a homogeneous membrane fraction and another one enriched in particulate inclusions. The latter exhibited a yellow-brown coloration and contained bodies lacking a delimiting membrane, which were characterised by a granular pattern and high electron density. The lipofuscin-like inclusion materials were rich in tripeptidyl peptidase 1, beta-glucuronidase, acid ceramidase and apolipoprotein D and contained proteins originating from diverse subcellular localisations. Here we show that human term placenta contains lipofuscin-like lysosomal inclusions, a phenomenon usually associated with senescence in postmitotic cells. These findings imply that a simple pelleting of a lysosomal lysate is not appropriate for the isolation of lysosomal membranes, as the inclusions tend to be sedimented with the membranes. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.febslet.2006.12.005"],["dc.identifier.isi","000243652900017"],["dc.identifier.pmid","17174955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/52132"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1873-3468"],["dc.relation.issn","0014-5793"],["dc.title","Characterisation of lipofuscin-like lysosomal inclusion bodies from human placenta"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","83"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","90"],["dc.bibliographiccitation.volume","422"],["dc.contributor.author","Schieweck, Oliver"],["dc.contributor.author","Damme, Markus"],["dc.contributor.author","Schroeder, Bernd"],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Luebke, Torben"],["dc.date.accessioned","2018-11-07T11:25:41Z"],["dc.date.available","2018-11-07T11:25:41Z"],["dc.date.issued","2009"],["dc.description.abstract","Until recently, a modest number of approx. 40 lysosomal membrane proteins had been identified and event fewer were characterized in their function. In a proteomic study, using lysosomal membranes from human placenta we identified several candidate lysosomal membrane proteins and proved the lysosomal localization of two of them. In the present study, we demonstrate the lysosomal localization of the mouse orthologue of the human Clorf85 protein, which has been termed kidney-predominant protein NCU-G1 (GenBank (R) accession number: AB027141). NCU-G1 encodes a 404 amino acid protein with a calculated molecular mass of 39 kDa. The bioinformatics analysis of its amino acid sequence suggests it is a type I transmembrane protein containing a single tyrosine-based consensus lysosomal sorting motif at position 400 within the 12-residue C-terminal tail. Its lysosomal localization was confirmed using immunofluorescence with a C-terminally His-tagged NCU-G1 and the lysosomal marker LAMP-1 (lysosome-associated membrane protein-1) as a reference. and by subcellular fractionation of mouse liver after a tyloxapol-induced density shift of the lysosomal fraction using all anti-NCU-G1 antiserum. In transiently transfected HT1080 and HeLa cells, the His-tagged NCU-G1 was detected in two molecular forms with apparent protein sizes of 70 and 80 kDa, and in mouse liver the endogenous wild-type NCU-G1 was detected as a 75 kDa protein. The remarkable difference between the apparent and the calculated molecular-masses of NCU-G1 was shown. by digesting the protein with N-glycosidase F, to be due to all extensive glycosylation. The lysosomal localization was impaired by mutational replacement of an alanine residue for the tyrosine residue within the Putative sorting, motif."],["dc.identifier.doi","10.1042/BJ20090567"],["dc.identifier.isi","000269023100009"],["dc.identifier.pmid","19489740"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56685"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.relation.issn","0264-6021"],["dc.title","NCU-G1 is a highly glycosylated integral membrane protein of the lysosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]