Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo
Protein complexes play a decisive role for lysosomal function. Here, the authors use cross-linking mass spectrometry and integrative modeling to investigate lysosomes and early endosomes; characterizing protein interactions, structures, and the cargo of flotillin-mediated endocytosis.
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-33951-0 |
| _version_ | 1828218046256250880 |
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| author | Jasjot Singh Hadeer Elhabashy Pathma Muthukottiappan Markus Stepath Martin Eisenacher Oliver Kohlbacher Volkmar Gieselmann Dominic Winter |
| author_facet | Jasjot Singh Hadeer Elhabashy Pathma Muthukottiappan Markus Stepath Martin Eisenacher Oliver Kohlbacher Volkmar Gieselmann Dominic Winter |
| author_sort | Jasjot Singh |
| collection | DOAJ |
| description | Protein complexes play a decisive role for lysosomal function. Here, the authors use cross-linking mass spectrometry and integrative modeling to investigate lysosomes and early endosomes; characterizing protein interactions, structures, and the cargo of flotillin-mediated endocytosis. |
| first_indexed | 2024-04-12T15:56:35Z |
| format | Article |
| id | doaj.art-daf33278d958445881e9a33767251849 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-12T15:56:35Z |
| publishDate | 2022-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-daf33278d958445881e9a337672518492022-12-22T03:26:20ZengNature PortfolioNature Communications2041-17232022-10-0113111810.1038/s41467-022-33951-0Cross-linking of the endolysosomal system reveals potential flotillin structures and cargoJasjot Singh0Hadeer Elhabashy1Pathma Muthukottiappan2Markus Stepath3Martin Eisenacher4Oliver Kohlbacher5Volkmar Gieselmann6Dominic Winter7Institute for Biochemistry and Molecular Biology, Medical Faculty, University of BonnDepartment of Protein Evolution, Max-Planck-Institute for Developmental BiologyInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of BonnMedical Proteome-Center, Medical Faculty, Ruhr-University BochumMedical Proteome-Center, Medical Faculty, Ruhr-University BochumInstitute for Bioinformatics and Medical Informatics, University of TübingenInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of BonnInstitute for Biochemistry and Molecular Biology, Medical Faculty, University of BonnProtein complexes play a decisive role for lysosomal function. Here, the authors use cross-linking mass spectrometry and integrative modeling to investigate lysosomes and early endosomes; characterizing protein interactions, structures, and the cargo of flotillin-mediated endocytosis.https://doi.org/10.1038/s41467-022-33951-0 |
| spellingShingle | Jasjot Singh Hadeer Elhabashy Pathma Muthukottiappan Markus Stepath Martin Eisenacher Oliver Kohlbacher Volkmar Gieselmann Dominic Winter Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo Nature Communications |
| title | Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo |
| title_full | Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo |
| title_fullStr | Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo |
| title_full_unstemmed | Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo |
| title_short | Cross-linking of the endolysosomal system reveals potential flotillin structures and cargo |
| title_sort | cross linking of the endolysosomal system reveals potential flotillin structures and cargo |
| url | https://doi.org/10.1038/s41467-022-33951-0 |
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