Schmidt, Bernhard

[["dc.bibliographiccitation.firstpage","3497"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3506"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Peters, Christoph"],["dc.contributor.author","Braun, Martin"],["dc.contributor.author","Weber, Birgit"],["dc.contributor.author","Wendland, Martin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1990"],["dc.description.abstract","Lysosomal acid phosphatase (LAP) is synthesized as a transmembrane protein with a short carboxy-terminal cytoplasmic tail of 19 amino acids, and processed to a soluble protein after transport to lysosomes. Deletion of the membrane spanning domain and the cytoplasmic tail converts LAP to a secretory protein, while deletion of the cytoplasmic tail as well as substitution of tyrosine 413 within the cytoplasmic tail against phenylalanine causes accumulation at the cell surface. A chimeric polypeptide, in which the cytoplasmic tail of LAP was fused to the ectoplasmic and transmembrane domain of hemagglutinin is rapidly internalized and tyrosine 413 of the LAP tail is essential for internalization of the fusion protein. A chimeric polypeptide, in which the membrane spanning domain and cytoplasmic tail of LAP are fused to the ectoplasmic domain of the Mr 46 kd mannose 6-phosphate receptor, is rapidly transported to lysosomes, whereas wild type receptor is not transported to lysosomes. We conclude that a tyrosine containing endocytosis signal in the cytoplasmic tail of LAP is necessary and sufficient for targeting to lysosomes."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61024"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","endocytosis signal;intemalization; lysosomes; targeting"],["dc.subject.ddc","610"],["dc.title","Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4391"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","4399"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Lehmann, Lutz E."],["dc.contributor.author","Eberle, Wolfgang"],["dc.contributor.author","Krull, Sabine"],["dc.contributor.author","Prill, Volkmar"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Sander, Chris"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Peters, Christoph"],["dc.date.accessioned","2019-07-10T08:12:45Z"],["dc.date.available","2019-07-10T08:12:45Z"],["dc.date.issued","1992"],["dc.description.abstract","Lysosomal acid phosphatase (LAP) is rapidly internalized from the cell surface due to a tyrosine-containing internalization signal in its 19 amino acid cytoplasmic tail. Measuring the internalization of a series of LAP cytoplasmic tail truncation and substitution mutants revealed that the N-terminal 12 amino acids of the cytoplasmic tail are sufficient for rapid endocytosis and that the hexapeptide 411-PGYRHV416 is the tyrosinecontaining internalization signal. Truncation and substitution mutants of amino acid residues following Val416 can prevent internalization even though these residues do not belong to the internalization signal. It was shown recently that part of the LAP cytoplasmic tail peptide corresponding to 410-PPGY413 forms a wellordered β turn structure in solution. Two-dimensional NNMR spectroscopy of two modified LAP tail peptides, in which the single tyrosine was substituted either by phenylalanine or by alanine, revealed that the tendency to form a β turn is reduced by 25% in the phenylalaninecontaining peptide and by ~ 50% in the alaninecontaining mutant peptide. Our results suggest, that in the short cytoplasmic tail of LAP tyrosine is required for stabilization of the tight turn and that the aromatic ring system of the tyrosine residue is a contact point to the putative cytoplasmic receptor."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3439"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61028"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","2D-NMR; endocytosis; internalization signal; lysosomal acid phosphatase"],["dc.subject.ddc","610"],["dc.title","The internalization signal in the cytoplasmic tail of lysosomal acid phosphatase consists of the hexapeptide PGYRHV"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]