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Inhibition of iron uptake by ferristatin II is exerted through internalization of DMT1 at the plasma membrane
Author(s) -
Yanatori Izumi,
Yasui Yumiko,
Noguchi Yumiko,
Kishi Fumio
Publication year - 2015
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.10403
Subject(s) - internalization , dmt1 , transferrin receptor , endocytosis , transferrin , chemistry , dynamin , cytosol , membrane , microbiology and biotechnology , biophysics , biochemistry , receptor , transporter , biology , gene , enzyme
Abstract Ferristatin II, discovered as an iron transport inhibitor, promotes the internalization and degradation of transferrin receptor 1 (TfR1). DMT1, which mediates iron transport across cell membranes, is located at the plasma membrane of enterocytes and imports dietary iron into the cytosol. TfR1 is not directly engaged in the intestinal absorption of free iron, and iron uptake by DMT1 is attenuated by ferristatin II treatment. In this study, we found another function for ferristatin II in iron uptake. Ferristatin II did not cause degradation of DMT1 but did induce DMT1 internalization from the plasma membrane. Dynasore, a small molecule inhibitor of dynamin, did not inhibit this internalization by ferristatin II, which might occur via a clathrin‐independent pathway.

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