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Nutrient-regulated control of lysosome function by signaling lipid conversion
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ebner, Michael | - |
dc.contributor.author | Puchkov, Dmytro | - |
dc.contributor.author | Lopez-Ortega, Orestes | - |
dc.contributor.author | Muthukottiappan, Pathma | - |
dc.contributor.author | Su, Yanwei | - |
dc.contributor.author | Schmied, Christopher | - |
dc.contributor.author | Zillmann, Silke | - |
dc.contributor.author | Nikonenko, Iryna | - |
dc.contributor.author | Koddebusch, Jochen | - |
dc.contributor.author | Dornan, Gillian L. | - |
dc.contributor.author | Lucht, Max T. | - |
dc.contributor.author | Koka, Vonda | - |
dc.contributor.author | Jang, Wonyul | - |
dc.contributor.author | Koch, Philipp Alexander | - |
dc.contributor.author | Wallroth, Alexander | - |
dc.contributor.author | Lehmann, Martin | - |
dc.contributor.author | Bruegger, Britta | - |
dc.contributor.author | Pende, Mario | - |
dc.contributor.author | Winter, Dominic | - |
dc.contributor.author | Haucke, Volker | - |
dc.date.accessioned | 2024-04-22T05:14:33Z | - |
dc.date.available | 2024-04-22T05:14:33Z | - |
dc.date.created | 2024-04-22 | - |
dc.date.created | 2024-04-22 | - |
dc.date.created | 2024-04-22 | - |
dc.date.created | 2024-04-22 | - |
dc.date.issued | 2023-11 | - |
dc.identifier.citation | CELL, Vol.186 No.24, pp.5328-+ | - |
dc.identifier.issn | 0092-8674 | - |
dc.identifier.uri | https://hdl.handle.net/10371/199270 | - |
dc.description.abstract | Lysosomes serve dual antagonistic functions in cells by mediating anabolic growth signaling and the cata-bolic turnover of macromolecules. How these janus-faced activities are regulated in response to cellular nutrient status is poorly understood. We show here that lysosome morphology and function are reversibly controlled by a nutrient-regulated signaling lipid switch that triggers the conversion between peripheral motile mTOR complex 1 (mTORC1) signaling-active and static mTORC1-inactive degradative lysosomes clustered at the cell center. Starvation-triggered relocalization of phosphatidylinositol 4-phosphate (PI(4) P)-metabolizing enzymes reshapes the lysosomal surface proteome to facilitate lysosomal proteolysis and to repress mTORC1 signaling. Concomitantly, lysosomal phosphatidylinositol 3-phosphate (PI(3)P), which marks motile signaling-active lysosomes in the cell periphery, is erased. Interference with this PI(3)P/PI(4) P lipid switch module impairs the adaptive response of cells to altering nutrient supply. Our data unravel a key function for lysosomal phosphoinositide metabolism in rewiring organellar membrane dynamics in response to cellular nutrient status. | - |
dc.language | 영어 | - |
dc.publisher | CELL PRESS | - |
dc.title | Nutrient-regulated control of lysosome function by signaling lipid conversion | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.cell.2023.09.027 | - |
dc.citation.journaltitle | CELL | - |
dc.identifier.wosid | 001126092700001 | - |
dc.identifier.scopusid | 2-s2.0-85177554532 | - |
dc.citation.endpage | + | - |
dc.citation.number | 24 | - |
dc.citation.startpage | 5328 | - |
dc.citation.volume | 186 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Jang, Wonyul | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | BINDING PROTEIN CYCLE | - |
dc.subject.keywordPlus | CONTACT SITES | - |
dc.subject.keywordPlus | AMINO-ACIDS | - |
dc.subject.keywordPlus | AUTOPHAGY | - |
dc.subject.keywordPlus | ENDOSOME | - |
dc.subject.keywordPlus | MTORC1 | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | REVEALS | - |
dc.subject.keywordPlus | KINASE | - |
dc.subject.keywordPlus | SUBSTRATE | - |
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