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Pumping iron: the strange partnership of the hemochromatosis protein, a class I MHC homolog, with the transferrin receptor
Author(s) -
Enns Caroline A.
Publication year - 2001
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2001.020303.x
Subject(s) - transferrin receptor , biology , beta 2 microglobulin , transferrin , major histocompatibility complex , hereditary hemochromatosis , microbiology and biotechnology , receptor , mhc class i , hemochromatosis , transporter associated with antigen processing , transmembrane protein , biochemistry , genetics , immunology , antigen
People suffering from hereditary hemochromatosis (HH) can not regulate the uptake of iron properly and gradually accumulate iron in their body over their lifetime. The protein involved in HH, HFE, has been recently identified as a class I major histocompatibility complex (MHC) homolog. The wild‐type HFE associates and co‐traffics with the transferrin receptor (TfR). The mutation responsible for 83% of HH (C260Y) results in the failure of HFE to form a critical disulfide bond, bind β 2 microglobulin, bind TfR, and traffic to the cell surface. In non‐polarized cells, the partnership of HFE and TfR results in decreased iron uptake into cells. The mechanism whereby a class I MHC homolog modifies the function of a membrane receptor and how this dynamic complex of molecules regulates iron transport across intestinal epithelial cells is the subject of this review.