| Autor: |
Ramalingam, T. S., West, Anthony P., Lebrón, José A., Nangiana, Jasvinder S., Hogan, Thomas H., Enns, Caroline A., Bjorkman, Pamela J. |
| Předmět: |
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| Zdroj: |
Nature Cell Biology; Dec2000, Vol. 2 Issue 12, p953, 5p |
| Abstrakt: |
HFE, the protein that is mutated in hereditary haemochromatosis, binds to the transferrin receptor (TfR). Here we show that wild-type HFE and TfR localize in endosomes and at the basolateral membrane of a polarized duodenal epithelial cell line, whereas the primary haemochromatosis HFE mutant, and another mutant with impaired TfRbinding ability accumulate in the ER/Golgi and at the basolateral membrane, respectively. Levels of the ironstorage protein ferritin are greatly reduced and those of TfR are slightly increased in cells expressing wild-type HFE, but not in cells expressing either mutant. Addition of an endosomal-targeting sequence derived from the human low-density lipoprotein receptor (LDLR) to the TfRbinding-impaired mutant restores its endosomal localization but not ferritin reduction or TfR elevation. Thus, binding to TfR is required for transport of HFE to endosomes and regulation of intracellular iron homeostasis, but not for basolateral surface expression of HFE. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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