Dominic Winter
  • Institut für Biochemie und Molekularbiologie
  • lysosomes
  • proteomics
  • biochemistry
We are investigating the lysosome, the central lytic organelle of mammalian cells, with mass spectrometry-based proteomics and biochemistry/molecular biology approaches. For this purpose, we are developing novel mass spectrometry strategies for the enrichment of lysosomes and the characterization of lysosomal proteins. These methods include the relative and absolute quantification of proteins and posttranslational modifications, the identification of novel lysosomal proteins, the investigation of cell type- and organelle-specific proteins, the identification of protein-protein interactions, and the structural characterization of lysosomal proteins and protein complexes. We apply these techniques to the investigation of cell- and organ-specific differences in lysosomal protein composition, transcriptional regulation of lysosomal proteins, and the effect of pathological conditions on lysosomal composition and signaling.
Ausgewählte Publikationen

Ponnaiyan S, Akter F, Singh J, Winter D (2020) Comprehensive draft of the mouse embryonic fibroblast lysosomal proteome by mass spectrometry based proteomics. Scient Data 2020, 7 (1), 68

Müller T and Winter D (2017) Systematic Evaluation of Protein Reduction and Alkylation Reveals Massive Unspecific Side Effects by Iodine-containing Reagents. Mol Cell Prot 2017, 16:1173-1187

Singh S*, Winter D*, Kirchner M*, Chauchan R*, Ahmed S, Ozlu N, Tzur A, Steen JA and Steen H (2014) Co-regulation proteomics reveals substrates and mechanisms of APC/C-dependent degradation. EMBO Journal 2014, Feb 18;33(4):385-99. *shared first authorship

Wang X, Winter D, Ashrafi G, Schlehe J, Wong YL, Selkoe D, Rice S, Steen J, Lavoie MJ and Schwarz TL (2011) PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility. Cell 2011, 147:893-906

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