Manganese-induced trafficking and turnover of the cis-Golgi glycoprotein GPP130.

Molecular Biology of the Cell
Somshuvra MukhopadhyayAdam D Linstedt

Abstract

Manganese is an essential element that is also neurotoxic at elevated exposure. However, mechanisms regulating Mn homeostasis in mammalian cells are largely unknown. Because increases in cytosolic Mn induce rapid changes in the localization of proteins involved in regulating intracellular Mn concentrations in yeast, we were intrigued to discover that low concentrations of extracellular Mn induced rapid redistribution of the mammalian cis-Golgi glycoprotein Golgi phosphoprotein of 130 kDa (GPP130) to multivesicular bodies. GPP130 was subsequently degraded in lysosomes. The Mn-induced trafficking of GPP130 occurred from the Golgi via a Rab-7-dependent pathway and did not require its transit through the plasma membrane or early endosomes. Although the cytoplasmic domain of GPP130 was dispensable for its ability to respond to Mn, its lumenal stem domain was required and it had to be targeted to the cis-Golgi for the Mn response to occur. Remarkably, the stem domain was sufficient to confer Mn sensitivity to another cis-Golgi protein. Our results identify the stem domain of GPP130 as a novel Mn sensor in the Golgi lumen of mammalian cells.

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Citations

May 15, 2013·Journal of Molecular Medicine : Official Organ of the Gesellschaft Deutscher Naturforscher Und Ärzte·Somshuvra Mukhopadhyay, Adam D Linstedt
Dec 29, 2010·Proceedings of the National Academy of Sciences of the United States of America·Somshuvra Mukhopadhyay, Adam D Linstedt
Jun 14, 2013·Molecular Biology of the Cell·Somshuvra MukhopadhyayAdam D Linstedt
Mar 17, 2012·Journal of Cell Science·Timothy Jarvela, Adam D Linstedt
Nov 15, 2013·Molecular Biology of the Cell·Timothy Jarvela, Adam D Linstedt
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Methods Mentioned

BETA
glycosylation
transfections
transfection
GTPase

Software Mentioned

ImageJ
Imaging Suite
RGB
ImageGauge
NCSS

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