{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Massa Lopez D"],"funding":["Deutsche Forschungsgemeinschaft","European Commission"],"pagination":["e50025"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6819133"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8"],"pubmed_abstract":["Lysosomes are major sites for intracellular, acidic hydrolase-mediated proteolysis and cellular degradation. The export of low-molecular-weight catabolic end-products is facilitated by polytopic transmembrane proteins mediating secondary active or passive transport. A number of these lysosomal transporters, however, remain enigmatic. We present a detailed analysis of MFSD1, a hitherto uncharacterized lysosomal family member of the major facilitator superfamily. MFSD1 is not N-glycosylated. It contains a dileucine-based sorting motif needed for its transport to lysosomes. <i>Mfsd1</i> knockout mice develop splenomegaly and severe liver disease. Proteomics of isolated lysosomes from <i>Mfsd1</i> knockout mice revealed GLMP as a critical accessory subunit for MFSD1. MFSD1 and GLMP physically "],"journal":["eLife"],"pubmed_title":["The lysosomal transporter MFSD1 is essential for liver homeostasis and critically depends on its accessory subunit GLMP."],"pmcid":["PMC6819133"],"funding_grant_id":["DA 1785-1","607446 Euroclast"],"pubmed_authors":["Massa Lopez D","Linhorst A","Hermanns-Borgmeyer I","Thelen M","Stahl F","Thiel C","Eskild W","Damme M","Sylvester M","Lullmann-Rauch R","Saftig P"],"additional_accession":[]},"is_claimable":false,"name":"The lysosomal transporter MFSD1 is essential for liver homeostasis and critically depends on its accessory subunit GLMP.","description":"Lysosomes are major sites for intracellular, acidic hydrolase-mediated proteolysis and cellular degradation. The export of low-molecular-weight catabolic end-products is facilitated by polytopic transmembrane proteins mediating secondary active or passive transport. A number of these lysosomal transporters, however, remain enigmatic. We present a detailed analysis of MFSD1, a hitherto uncharacterized lysosomal family member of the major facilitator superfamily. MFSD1 is not N-glycosylated. It contains a dileucine-based sorting motif needed for its transport to lysosomes. <i>Mfsd1</i> knockout mice develop splenomegaly and severe liver disease. Proteomics of isolated lysosomes from <i>Mfsd1</i> knockout mice revealed GLMP as a critical accessory subunit for MFSD1. MFSD1 and GLMP physically ","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2026-04-14T09:20:45.863Z","creation":"2019-11-07T08:08:22Z"},"accession":"S-EPMC6819133","cross_references":{"pubmed":["31661432"],"doi":["10.7554/eLife.50025"]}}