Multidrug and toxin extrusion protein (MATE)

Multidrug and toxin extrusion protein (MATE) refers to a family of membrane transporters found across bacteria, archaea, and eukaryotes, notable for actively exporting endogenous and exogenous organic cations and xenobiotics such as drugs and toxins from the cytoplasm into bile, urine, or the extracellular space[1][2][3][4][7]. They use transmembrane sodium or proton gradients to drive efflux and thereby play a crucial role in renal and hepatic drug clearance, as well as cellular detoxification[2][4]. Human MATE proteins (notably SLC47A1/MATE1, SLC47A2/MATE2, and MATE2-K) are highly expressed in kidney and liver, localizing to apical membranes where they participate in active secretion of many clinically relevant drugs including metformin, cimetidine, cephalosporins, and antivirals[2][3][7]. Variants in these genes can alter drug pharmacokinetics and response, making them relevant for personalized medicine[4]. MATE proteins also contribute to multidrug resistance in bacteria and cancer, influencing xenobiotic disposition and therapeutic outcomes[1][7]. Structural studies predict 12-13 transmembrane helices with conserved mechanisms for substrate binding and antiport function[1][4][6].

Other names

Multi-antimicrobial extrusion proteinmultidrug and toxic compound extrusion proteinMATE transporterSLC47 family memberNorM (prototypic bacterial member)

Drugs are transported via proton-coupled or sodium-coupled antiport mechanisms, leading to active efflux of cations and xenobiotics from cells; drug resistance occurs through extrusion from target tissues/cells