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The family of proton-coupled metal ion transporters are responsible for movements of divalent cations, particularly ferrous and manganese ions, across the cell membrane (DMT1) and across endosomal (DMT1) or lysosomal/phagosomal membranes (NRAMP1), dependent on proton transport. Both proteins appear to have 12 TM regions and cytoplasmic N- and C- termini. NRAMP1 is involved in antimicrobial action in macrophages, although it’s precise mechanism is undefined. Facilitated diffusion of divalent cations into phagosomes may increase intravesicular free radicals to damage the pathogen. Alternatively, export of divalent cations from the phagosome may deprive the pathogen of essential enzyme cofactors. DMT1 is more widely expressed and appears to assist in divalent cation assimilation from the diet, as well as in phagocytotic cells.
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
NRAMP1 (SLC11A1) Show »
Divalent metal transporter 1 (SLC11A2) Show »
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Further Reading Show »
Li, X; Yang, Y; Zhou, F; Zhang, Y; Lu, H; Jin, Q; Gao, L. (2011) SLC11A1 (NRAMP1) polymorphisms and tuberculosis susceptibility: updated systematic review and meta-analysis. PLoS ONE, 6 (1): e15831. [PMID:21283567]
Mackenzie, B; Hediger, MA. (2004) SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1. Pflugers Arch., 447 (5): 571-9. [PMID:14530973]
Nevo, Y; Nelson, N. (2006) The NRAMP family of metal-ion transporters. Biochim. Biophys. Acta, 1763 (7): 609-20. [PMID:16908340]
References Show »
1. Gunshin, H; Mackenzie, B; Berger, UV; Gunshin, Y; Romero, MF; Boron, WF; Nussberger, S; Gollan, JL; Hediger, MA. (1997) Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature, 388 (6641): 482-8. [PMID:9242408]