The lysosomal transporter MFSD1 is essential for liver homeostasis and critically depends on its accessory subunit GLMP
Identifieur interne : 003F91 ( Main/Exploration ); précédent : 003F90; suivant : 003F92The lysosomal transporter MFSD1 is essential for liver homeostasis and critically depends on its accessory subunit GLMP
Auteurs : David Massa L Pez [Allemagne] ; Melanie Thelen [Allemagne] ; Felix Stahl [Allemagne] ; Christian Thiel [Allemagne] ; Arne Linhorst [Allemagne] ; Marc Sylvester [Allemagne] ; Irm Hermanns-Borgmeyer [Allemagne] ; Renate Lüllmann-Rauch [Allemagne] ; Winnie Eskild [Norvège] ; Paul Saftig [Allemagne] ; Markus Damme [Allemagne]Source :
- eLife [ 2050-084X ] ; ????.
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.
Url:
DOI: 10.7554/eLife.50025
PubMed: 31661432
PubMed Central: 6819133
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>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. <italic>Mfsd1</italic>
knockout mice develop splenomegaly and severe liver disease. Proteomics of isolated lysosomes from <italic>Mfsd1</italic>
knockout mice revealed GLMP as a critical accessory subunit for MFSD1. MFSD1 and GLMP physically interact. GLMP is essential for the maintenance of normal levels of MFSD1 in lysosomes and vice versa. <italic>Glmp</italic>
knockout mice mimic the phenotype of <italic>Mfsd1</italic>
knockout mice. Our data reveal a tightly linked MFSD1/GLMP lysosomal membrane protein transporter complex.</p>
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