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A more recent version of this article appeared on March 2, 2007
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Papers In Press, published online ahead of print January 2, 2007
J. Biol. Chem, 10.1074/jbc.M610127200
Submitted on October 30, 2006
Revised on December 19, 2006
Accepted on January 2, 2007

The cytoplasmic domain of transferrin receptor 2 dictates its stability and response to holo-transferrin in HEP3B cells

Juxing Chen and Caroline A. Enns

Cell and Developmental Biology, Oregon Health & Science University, Portland, OR 97239

Corresponding Author: ennsca{at}ohsu.edu

Transferrin receptor 2 (TfR2) is homolog of transferrin receptor 1 (TfR1), the receptor responsible for the uptake of iron-loaded transferrin (holo-Tf) into cells. Unlike the ubiquitous TfR1, TfR2 is predominantly expressed in the liver. Mutations in TfR2 gene cause a rare autosomal recessive form of the iron overload disease, hereditary hemochromatosis. Previous studies demonstrated that holo-Tf increases TfR2 levels by stabilizing TfR2 at the protein level. In this study, we constructed two chimeras one of which had the cytoplasmic domain of TfR2 and the remaining portion of TfR1 and the other with the cytoplasmic and transmembrane domain of TfR1 joined to the ectodomain of TfR2. Similar to TfR2, the levels of the chimera containing only the cytoplasmic domain of TfR2 increased in a time- and dose-dependent manner after addition of holo-Tf to the medium. The half-life of the chimera increased 2.7 fold in cells exposed to holo-Tf like the endogenous TfR2 in HepG2 cells. Like TfR2 and unlike TfR1, the levels of the chimera did not respond to intracellular iron content. These results suggest that while holo-Tf binding to the ectodomain is necessary, the cytoplasmic domain of TfR2 is largely responsible for its stabilization by holo-Tf.


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