{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lee C"],"funding":["NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["2060-2075"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12246789"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(10)"],"pubmed_abstract":["Lysosomes, central hydrolytic organelles, are regulated by ion flow, including calcium and protons, via transporters and channels to maintain an acidified lumen for hydrolytic activity. TRPML1, a lysosomal ion channel, effluxes cations upon activation, promoting rapid conjugation of ATG8 proteins to the lysosomal membrane in a process known as conjugation of ATG8 to single membranes (CASM). However, our understanding of how TRPML1 activation reorganizes the lysosomal proteome is poorly understood. Here, we identify DMXL1 as a key regulator of lysosomal homeostasis through quantitative proteomics of lysosomes during TRPML1 activation by the agonist MLSA5. DMXL1 is recruited to lysosomes and Salmonella-containing vacuoles, both in a CASM-dependent manner. As the mammalian ortholog of yeast R"],"journal":["Nature structural & molecular biology"],"pubmed_title":["DMXL1 promotes recruitment of V1-ATPase to lysosomes upon TRPML1 activation."],"pmcid":["PMC12246789"],"funding_grant_id":["R01 GM132129","R01 NS083524","R01 NS110395"],"pubmed_authors":["Harper JW","Lee C","Fu T","Moran MM","Bresnahan T","Paulo JA","Helaine S","Gonzalez-Lozano MA","Niday Z","Eldridge MJG","Del Camino D"],"additional_accession":[]},"is_claimable":false,"name":"DMXL1 promotes recruitment of V1-ATPase to lysosomes upon TRPML1 activation.","description":"Lysosomes, central hydrolytic organelles, are regulated by ion flow, including calcium and protons, via transporters and channels to maintain an acidified lumen for hydrolytic activity. TRPML1, a lysosomal ion channel, effluxes cations upon activation, promoting rapid conjugation of ATG8 proteins to the lysosomal membrane in a process known as conjugation of ATG8 to single membranes (CASM). However, our understanding of how TRPML1 activation reorganizes the lysosomal proteome is poorly understood. Here, we identify DMXL1 as a key regulator of lysosomal homeostasis through quantitative proteomics of lysosomes during TRPML1 activation by the agonist MLSA5. DMXL1 is recruited to lysosomes and Salmonella-containing vacuoles, both in a CASM-dependent manner. As the mammalian ortholog of yeast R","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-11T05:06:01.119Z","creation":"2026-06-11T03:08:24.35Z"},"accession":"S-EPMC12246789","cross_references":{"pubmed":["40527988"],"doi":["10.1038/s41594-025-01581-x"]}}