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Journal Article

Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo

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Elhabashy,  H       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Singh, J., Elhabashy, H., Muthukottiappan, P., Stepath, M., Eisenacher, M., Kohlbacher, O., et al. (2022). Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo. Nature Communications, 13(1): 6212. doi:10.1038/s41467-022-33951-0.


Cite as: https://hdl.handle.net/21.11116/0000-000B-593A-1
Abstract
Lysosomes are well-established as the main cellular organelles for the degradation of macromolecules and emerging as regulatory centers of metabolism. They are of crucial importance for cellular homeostasis, which is exemplified by a plethora of disorders related to alterations in lysosomal function. In this context, protein complexes play a decisive role, regulating not only metabolic lysosomal processes but also lysosome biogenesis, transport, and interaction with other organelles. Using cross-linking mass spectrometry, we analyze lysosomes and early endosomes. Based on the identification of 5376 cross-links, we investigate protein-protein interactions and structures of lysosome- and endosome-related proteins. In particular, we present evidence for a tetrameric assembly of the lysosomal hydrolase PPT1 and a heterodimeric structure of FLOT1/FLOT2 at lysosomes and early endosomes. For FLOT1-/FLOT2-positive early endosomes, we identify >300 putative cargo proteins and confirm eleven substrates for flotillin-dependent endocytosis, including the latrophilin family of adhesion G protein-coupled receptors.