NDLI: Essential role for Atox1 in the copper-mediated intracellular trafficking of the Menkes ATPase.

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Essential role for Atox1 in the copper-mediated intracellular trafficking of the Menkes ATPase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Prohaska, Joseph Gitlin, Jonathan D. Hamza, Iqbal
Description	Author Affiliation: Hamza I ( Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA.);
Abstract	The metallochaperone Atox1 directly interacts with the copper-transporting ATPases and plays a critical role in perinatal copper homeostasis. To determine the cell biological mechanisms of Atox1 function, intracellular copper metabolism, and Menkes ATPase abundance, localization and trafficking were examined in immortalized fibroblast cell lines derived from Atox1(+/+) and Atox1(-/-) embryos. Consistent with the proposed role for Atox1 in copper delivery to the secretory pathway, a marked increase in intracellular copper content secondary to impaired copper efflux was observed in Atox1-deficient cells. Although the localization of the Menkes ATPase was identical in Atox1(+/+) and Atox1(-/-) cells under conditions of equivalent intracellular copper content, a significant impairment in copper-mediated Menkes ATPase trafficking was observed in the absence of Atox1. When quantitative confocal immunofluorescence was used, significant differences in the time and dose-dependent trafficking of the Menkes ATPase from the Golgi compartment in response to copper were observed between Atox1(+/+) and Atox1(-/-) cells. These data reveal an essential role for Atox1 in establishing the threshold for copper-dependent movement of the copper-transporting ATPases within the secretory compartment and that, in the absence of Atox1, this movement alone is not sufficient to restore normal copper efflux. Taken together, these findings provide a cell biological model for the role of this metallochaperone under the physiological conditions of copper limitation in mammalian cells.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphatases Metabolism Cation Transport Proteins Physiology Copper Molecular Chaperones Recombinant Fusion Proteins Animals Cell Line Cells, Cultured Dose-Response Relationship, Drug Fibroblasts Image Processing, Computer-Assisted Immunoblotting Mice Microscopy, Confocal Microscopy, Fluorescence Protein Transport Retroviridae Genetics Spectrophotometry, Atomic Time Factors Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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