化学
伴侣(临床)
转铁蛋白
细胞生物学
金属蛋白
细胞内
铁转运蛋白
缺铁
生物物理学
血红素
作者
Haifeng Shi,Krisztina Z. Bencze,Timothy L. Stemmler,Caroline C. Philpott
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2008-05-30
卷期号:320 (5880): 1207-1210
被引量:420
标识
DOI:10.1126/science.1157643
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.
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