SGD Paper 
Lauer Junior CM, et al. (2008) The Pmr1 protein, the major yeast Ca2+-ATPase in the Golgi, regulates intracellular levels of the cadmium ion. FEMS Microbiol Lett 285(1):79-88
Abstract: Cadmium is a nonessential, highly toxic heavy metal that shows ionic properties similar to calcium. These ionic similarities imply that the cadmium ion, Cd(2+), is a calcium ion, Ca(2+), receptor-agonist, affecting the same biochemical pathways involved in Ca(2+) homeostasis. In the yeast Saccharomyces cerevisiae, the PMC1 and PMR1 genes encode vacuolar and Golgi Ca(2+)-ATPases, respectively. The PMR1 protein product Pmr1p is involved in both Ca(2+) and Mn(2+) homeostasis. This study investigated the importance of Pmc1p and Pmr1p for Cd(2+) cellular detoxification. Using the standard techniques of yeast molecular research and a multielemental procedure named particle-induced X-ray emission, Pmr1p was identified as a protein that directly participates in the detoxification of Cd(2+), possibly through the secretory pathway. The results allow us to posit a model of Cd(2+) detoxification where Pmr1p has a central role in cell survival in a Cd(2+)-rich environment.
| Status: Published | Type: Journal Article | PubMed ID: 18510555 |
Topics addressed in this paper
Number of different genes curated to this paper: 2
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