Mitoferrin 1 Rabbit Polyclonal Antibody

Function :
The molecular details of iron trafficking for heme and Iron-sulfur cluster synthesis are still unclear, however, Mitoferrin-1 has been shown to form oligomeric complexes with the ATP-binding cassette transporter ABCB10 and Ferrochelatase (or protoporphyrin ferrochelatase). Furthermore, ABC10 binding enhances the stability and functionality of Mfrn1, suggesting that transcriptional and post-translational mechanisms further regulate cellular and mitochondrial iron homeostasis. Recombinant Mfrn1 in vitro has micromolar affinity for the following first-row transition metals: iron (II), manganese (II), cobalt (II), and nickel (II). Mfrn1 iron transport was reconstituted in proteoliposomes, where the protein was also able to transport manganese, cobalt, copper, and zinc, yet it discriminated against nickel, despite the aforementioned affinity. Notably, Mfrn1 appears to transport free iron ions as opposed to any sort of chelated iron complex. Additionally, Mfrn1 selects against divalent alkali ions. Mfrn1 and its paralog Mfrn2 have complementary functionalities, though the precise relationship is still uncertain. For example, heme production is restored by expression of Mfrn2 in cells silenced for Mfrn1 and by ectopic expression of Mfrn1 in nonerythroid cells silenced for Mfrn2, where Mfrn1 accumulates due to an increased protein half-life. In contrast, ectopic expression of Mfrn2 failed to restore heme product in erythroid cells silenced for Mfrn1 because Mfrn2 was unable to accumulate in mitochondria.