Journal
JOURNAL OF CELL BIOLOGY
Volume 166, Issue 3, Pages 325-335Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200401157
Keywords
zinc; transport; cation diffusion facilitator; endoplasmic reticulum; unfolded
Categories
Funding
- NIGMS NIH HHS [R01 GM056285, F32 GM020545, F32 GM020545-02, GM56285, R01 GM069786, F32 GM020545-01, GM69786] Funding Source: Medline
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In this report, we show that zinc is required for endoplasmic reticulum function in Saccharomyces cerevisiae. Zinc deficiency in this yeast induces the unfolded protein response (UPR), a system normally activated by unfolded ER proteins. Msc2, a member of the cation diffusion facilitator (CDF) family of metal ion transporters, was previously implicated in zinc homeostasis. Our results indicate that Msc2 is one route of zinc entry into the ER. Msc2 localizes to the ER when expressed at normal levels. UPR induction in low zinc is exacerbated in an msc2 mutant. Genetic and biochemical evidence indicates that this UPR induction is due to genuine ER dysfunction. Notably, we found that ER-associated protein degradation is defective in zinc-limited msc2 mutants. We also show that the vacuolar CDF proteins Zrc1 and Cot1 are other pathways of ER zinc acquisition. Finally, zinc deficiency up-regulates the mammalian ER stress response indicating a conserved requirement for zinc in ER function among eukaryotes.
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