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Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis
Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis
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Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis
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Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis
Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis

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Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis
Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis
Journal Article

Ferroportin Metal Efflux Proteins Function in Iron and Cobalt Homeostasis in Arabidopsis

2009
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Overview
Relatively little is known about how metals such as iron are effluxed from cells, a necessary step for transport from the root to the shoot. Ferroportin (FPN) is the sole iron efflux transporter identified to date in animals, and there are two closely related orthologs in Arabidopsis thaliana, IRON REGULATED1 (IREG1/FPN1) and IREG2/FPN2. FPN1 localizes to the plasma membrane and is expressed in the stele, suggesting a role in vascular loading; FPN2 localizes to the vacuole and is expressed in the two outermost layers of the root in response to iron deficiency, suggesting a role in buffering metal influx. Consistent with these roles, fpn2 has a diminished iron deficiency response, whereas fpn1 fpn2 has an elevated iron deficiency response. Ferroportins also play a role in cobalt homeostasis; a survey of Arabidopsis accessions for ionomic phenotypes showed that truncation of FPN2 results in elevated shoot cobalt levels and leads to increased sensitivity to the metal. Conversely, loss of FPN1 abolishes shoot cobalt accumulation, even in the cobalt accumulating mutant frd3. Consequently, in the fpn1 fpn2 double mutant, cobalt cannot move to the shoot via FPN1 and is not sequestered in the root vacuoles via FPN2; instead, cobalt likely accumulates in the root cytoplasm causing fpn1 fpn2 to be even more sensitive to cobalt than fpn2 mutants.