{"id":28,"date":"2026-07-01T08:15:48","date_gmt":"2026-07-01T08:15:48","guid":{"rendered":"https:\/\/cellbiology-dev.i-med.ac.at\/?page_id=28"},"modified":"2026-07-20T09:09:17","modified_gmt":"2026-07-20T09:09:17","slug":"the-stasyk-laboratory","status":"publish","type":"page","link":"https:\/\/cellbiology-dev.i-med.ac.at\/index.php\/the-stasyk-laboratory\/","title":{"rendered":"The Stasyk Laboratory"},"content":{"rendered":"
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The Stasyk Laboratory: Molecular architecture of native lysosomal protein assemblies<\/h1>\n\n\n\n

Lysosomes are intracellular signaling platforms that govern cell growth, division and differentiation. Although our knowledge of the molecular mechanisms of the sensing of essential nutrients has advanced significantly, we still lack information on the interplay between the numerous components of sensing and signaling machineries. The LAMTOR\/Ragulator complex is a crucial regulator of lysosomal mTORC1, MAPK and AMPK signaling. Via the BORC complex, LAMTOR also coordinates lysosome biogenesis. The existence of distinct LAMTOR complexes on lysosomes raises questions on how anabolic and catabolic signaling, lysosomal biogenesis and positioning are coordinated.<\/p>\n\n\n\n

We are aiming to identify all LAMTOR- and BORC-associated protein assemblies on intact lysosomes and to obtain evidence for direct and endogenous protein-protein interactions. We are applying cross-linking mass spectrometry (XL-MS) in combination with subcellular fractionation to understand the molecular architectures of the protein complexes under different physiological conditions. Our approach captures native endogenous protein interactions using a chemical cross-linker that is reactive towards specific amino-acid side chains that are in close spatial proximity.<\/p>\n\n\n\n

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Publications<\/h2>\n\n\n\n

PubMed<\/a>, Google Scholar<\/a>, ORCID<\/a><\/p>\n\n\n\n