A cytosolic iron chaperone that delivers iron to ferritin

被引：404

作者：

Shi, Haifeng ^{[1
]}

Bencze, Krisztina Z. ^{[2
]}

Stemmler, Timothy L. ^{[2
]}

Philpott, Caroline C. ^{[1
]}

机构：

[1] NIDDKD, Liver Dis Branch, NIH, Bethesda, MD 20892 USA

[2] Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA

来源：

SCIENCE | 2008年 / 320卷 / 5880期

关键词：

D O I：

10.1126/science.1157643

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Ferritins are the main iron storage proteins found in animals, plants, and bacteria. The capacity to store iron in ferritin is essential for life in mammals, but the mechanism by which cytosolic iron is delivered to ferritin is unknown. Human ferritins expressed in yeast contain little iron. Human poly (rC)- binding protein 1 ( PCBP1) increased the amount of iron loaded into ferritin when expressed in yeast. PCBP1 bound to ferritin in vivo and bound iron and facilitated iron loading into ferritin in vitro. Depletion of PCBP1 in human cells inhibited ferritin iron loading and increased cytosolic iron pools. Thus, PCBP1 can function as a cytosolic iron chaperone in the delivery of iron to ferritin.

引用

页码：1207 / 1210

页数：4

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