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Transferrin-mediated cellular iron delivery
#MMPMID23046645
Luck AN
; Mason AB
Curr Top Membr
2012[]; 69
(?): 3-35
PMID23046645
show ga
Essential to iron homeostasis is the transport of iron by the bilobal protein
human serum transferrin (hTF). Each lobe (N- and C-lobe) of hTF forms a deep
cleft which binds a single Fe(3+). Iron-bearing hTF in the blood binds tightly to
the specific transferrin receptor (TFR), a homodimeric transmembrane protein.
After undergoing endocytosis, acidification of the endosome initiates the release
of Fe(3+) from hTF in a TFR-mediated process. Iron-free hTF remains tightly bound
to the TFR at acidic pH; following recycling back to the cell surface, it is
released to sequester more iron. Efficient delivery of iron is critically
dependent on hTF/TFR interactions. Therefore, identification of the pH-specific
contacts between hTF and the TFR is crucial. Recombinant protein production has
enabled deconvolution of this complex system. The studies reviewed herein support
a model in which pH-induced interrelated events control receptor-stimulated iron
release from each lobe of hTF.
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