Copper chaperones: Personal escorts for metal ions
Copper chaperones: Personal escorts for metal ions
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DOI：
10.1023/a:1021202119942
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发表时间：
2002-10-01
影响因子：
3
通讯作者：
Culotta, VC
中科院分区：
文献类型：
--
作者：
Field, LS;Luk, E;Culotta, VC
铜是参与氧化还原化学的许多酶的重要辅因子，几乎所有生物体都必须积累微量的铜才能生存。然而，这种金属也可能是有毒的，许多有效的螯合和解毒铜的方法可以防止金属在细胞内自由循环。因此，铜金属酶面临着在缺乏可用铜的情况下获得其贵金属辅因子的挑战。为了克服这一困境，所有真核生物都进化出了一个细胞内铜结合蛋白家族，这些蛋白有助于为金属酶保留生物可利用的铜库，护送金属到适当的靶点，并直接转移铜离子。这些蛋白质被统称为“铜分子伴侣”。“通过对面包酵母酿酒酵母的分子遗传学研究，此类分子的鉴定成为可能。在这篇综述中，我们强调的结果，导致了一个新的范例，涉及铜分子伴侣的行动细胞内贩运铜。特别是，重点将放在ATX 1和CCS铜分子伴侣上，它们分别用于将铜传递到分泌途径和细胞质中的Cu/Zn超氧化物歧化酶。
Copper serves as the essential cofactor for a number of enzymes involved in redox chemistry and virtually all organisms must accumulate trace levels of copper in order to survive. However, this metal can also be toxic and a number of effective methods for sequestering and detoxifying copper prevent the metal from freely circulating inside a cell. Copper metalloenzymes are therefore faced with the challenge of acquiring their precious metal cofactor in the absence of available copper. To overcome this dilemma, all eukaryotic organisms have evolved with a family of intracellular copper binding proteins that help reserve a bioavailable pool of copper for the metalloenzymes, escort the metal to appropriate targets, and directly transfer the copper ion. These proteins have been collectively called "copper chaperones." The identification of such molecules has been made possible through molecular genetic studies in the bakers' yeast Saccharomyces cerevisiae. In this review, we highlight the findings that led to a new paradigm of intracellular trafficking of copper involving the action of copper chaperones. In particular, emphasis will be placed on the ATX1 and CCS copper chaperones that act to deliver copper to the secretory pathway and to Cu/Zn superoxide dismutase in the cytosol, respectively.