{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["301(7)"],"submitter":["Zhou Y"],"funding":["Graduate Research and Innovation Projects of Jiangsu Province","National Natural Science Foundation of China"],"pubmed_abstract":["The Rag GTPases play an important role in sensing amino acids and activating the target of rapamycin complex 1, a master regulator of cell metabolism. Previously, we have shown that GDP-bound RagA stimulates lysosome acidification and autophagic degradation, which are essential for young egg chamber survival under starvation in Drosophila. However, the underlying mechanism is unclear. Here, we demonstrate that the GDP-bound RagA breaks the physical interaction between cytosolic chaperonin-containing tailless complex polypeptide 1 (CCT) and vacuolar H+-ATPase (v-ATPase) subunit V1, and thus promotes the assembly of active v-ATPase and increases the lysosomal acidification. Consistently, knockdown of CCT complex components rescued the accumulation of defective autolysosomes in RagA RNAi. Mor"],"journal":["The Journal of biological chemistry"],"pagination":["110400"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12332402"],"repository":["biostudies-literature"],"pubmed_title":["Rag GTPases control lysosomal acidification by regulating v-ATPase assembly in Drosophila."],"pmcid":["PMC12332402"],"pubmed_authors":["Yang X","Fan W","Lu Y","Shen S","Zhou Y","Xu W","Wei Y","Cheng Y","Meng G"],"additional_accession":[]},"is_claimable":false,"name":"Rag GTPases control lysosomal acidification by regulating v-ATPase assembly in Drosophila.","description":"The Rag GTPases play an important role in sensing amino acids and activating the target of rapamycin complex 1, a master regulator of cell metabolism. Previously, we have shown that GDP-bound RagA stimulates lysosome acidification and autophagic degradation, which are essential for young egg chamber survival under starvation in Drosophila. However, the underlying mechanism is unclear. Here, we demonstrate that the GDP-bound RagA breaks the physical interaction between cytosolic chaperonin-containing tailless complex polypeptide 1 (CCT) and vacuolar H+-ATPase (v-ATPase) subunit V1, and thus promotes the assembly of active v-ATPase and increases the lysosomal acidification. Consistently, knockdown of CCT complex components rescued the accumulation of defective autolysosomes in RagA RNAi. Mor","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-05-01T08:35:19.032Z","creation":"2026-04-07T16:47:01.63Z"},"accession":"S-EPMC12332402","cross_references":{"pubmed":["40543592"],"doi":["10.1016/j.jbc.2025.110400"]}}