Major facilitator superfamily domain-containing protein 1 (MFSD1)

Major facilitator superfamily domain-containing protein 1 (MFSD1) is an atypical solute carrier of the major facilitator superfamily, primarily localized in lysosomal membranes. MFSD1 forms a stable complex with the accessory protein GLMP and acts as a selective uniporter for dipeptides containing lysine, arginine, or histidine. It facilitates export of dipeptides produced via lysosomal proteolysis into the cytoplasm, providing an alternative route for metabolic recycling and biosynthetic precursors when amino acid exporters are saturated. MFSD1 works independently of the lysosomal pH gradient, is specific for dipeptides, and is structurally distinct from canonical proton-coupled oligopeptide transporters. It is ubiquitously expressed and plays essential roles in liver homeostasis, cell migration, integrin recycling, and possibly immune cell development. Disruption of MFSD1 results in severe metabolic, hepatic, immunological, and proliferative abnormalities, highlighting its clinical relevance as a potential therapeutic and research target[1][2][3][4][5][6][7][8][9][10].

Other names

Lysosomal dipeptide transporter MFSD1SMAP4SLC72A1MinervaSmooth muscle cell-associated protein 4Major facilitator superfamily domain-containing protein 1FLJ14153UG0581B09

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