Lin S J, Pufahl R A, Dancis A, O'Halloran T V, Culotta V C
Division of Toxicological Sciences, Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Baltimore, Maryland 21205, USA.
J Biol Chem. 1997 Apr 4;272(14):9215-20.
The ATX1 gene of Saccharomyces cerevisiae was originally identified as a multi-copy suppressor of oxidative damage in yeast lacking superoxide dismutase. We now provide evidence that Atx1p helps deliver copper to the copper requiring oxidase Fet3p involved in iron uptake. atx1Delta null mutants are iron-deficient and are defective in the high affinity uptake of iron. These defects due to ATX1 inactivation are rescued by copper treatment, and the same has been reported for strains lacking either the cell surface copper transporter, Ctr1p, or the putative copper transporter in the secretory pathway, Ccc2p. Atx1p localizes to the cytosol, and our studies indicate that it functions as a carrier for copper that delivers the metal from the cell surface Ctr1p to Ccc2p and then to Fet3p within the secretory pathway. The iron deficiency of atx1 mutants is augmented by mutations in END3 blocking endocytosis, suggesting that a parallel pathway for intracellular copper trafficking is mediated by endocytosis. As additional evidence for the role of Atx1p in iron metabolism, we find that the gene is induced by the same iron-sensing trans-activator, Aft1p, that regulates CCC2 and FET3.
酿酒酵母的ATX1基因最初被鉴定为缺乏超氧化物歧化酶的酵母中氧化损伤的多拷贝抑制因子。我们现在提供证据表明,Atx1p有助于将铜传递给参与铁摄取的需铜氧化酶Fet3p。atx1Delta缺失突变体缺铁,并且在铁的高亲和力摄取方面存在缺陷。由ATX1失活导致的这些缺陷可通过铜处理得到挽救,对于缺乏细胞表面铜转运蛋白Ctr1p或分泌途径中假定的铜转运蛋白Ccc2p的菌株,也有相同的报道。Atx1p定位于细胞质中,我们的研究表明它作为铜的载体发挥作用,将金属从细胞表面的Ctr1p传递到Ccc2p,然后在分泌途径中传递到Fet3p。END3中阻断内吞作用的突变加剧了atx1突变体的缺铁现象,这表明细胞内铜运输的平行途径是由内吞作用介导的。作为Atx1p在铁代谢中作用的额外证据,我们发现该基因由调节CCC2和FET3的相同铁感应反式激活因子Aft1p诱导。