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J Biol Chem, Vol. 273, Issue 44, 28617-28624, October 30, 1998
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From the The ZRT1 gene encodes the transporter
responsible for high affinity zinc uptake in yeast. ZRT1 is
transcribed in zinc-limited cells and its transcription is repressed in
zinc-replete cells. In this report, we describe a second,
post-translational mechanism that regulates ZRT1 activity. In
zinc-limited cells, ZRT1 is a stable, N-glycosylated plasma
membrane protein. Exposure to high levels of extracellular zinc
triggers a rapid loss of ZRT1 uptake activity. Our results demonstrate
that this inactivation occurs through zinc-induced endocytosis of the
protein and its subsequent degradation in the vacuole. Mutations that
inhibit the internalization step of endocytosis also inhibited
zinc-induced ZRT1 inactivation and the major vacuolar proteases were
required to degrade ZRT1 in response to zinc. Furthermore,
immunofluorescence microscopy showed that ZRT1 is localized to the
plasma membrane in zinc-limited cells and that the protein is
transferred to the vacuole via an endosome-like compartment upon
exposure to zinc. ZRT1 inactivation is a relatively specific response
to zinc; cadmium and cobalt ions trigger the response but less
effectively than zinc. Moreover, zinc does not alter the stability of
several other plasma membrane proteins. Therefore, zinc-induced ZRT1
inactivation is a specific regulatory system to shut off zinc uptake
activity in cells exposed to high extracellular zinc levels thereby
preventing overaccumulation of this potentially toxic metal.
Nutritional Sciences Program, University of
Missouri-Columbia, Columbia, Missouri 65211 and the
§ Department of Biochemistry and Molecular Biology,
University of Minnesota-Duluth, Duluth, Minnesota 55812
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