Erythropoiesis and Iron Sulfur Cluster Biogenesis.pdfVIP

Erythropoiesis and Iron Sulfur Cluster Biogenesis.pdf

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Erythropoiesis and Iron Sulfur Cluster Biogenesis.pdf

Hindawi Publishing Corporation Advances in Hematology Volume 2010, Article ID 329394, 8 pages doi:10.1155/2010/329394 Review Article Erythropoiesis and Iron Sulfur Cluster Biogenesis Hong Ye and Tracey A. Rouault Molecular Medicine Program, Eunice Kennedy Shriver National Institutes of Child Health and Human Development at (NIH), 9000 Rockville Pike, Bethesda, MD 20892, USA Correspondence should be addressed to Tracey A. Rouault, rouault@ Received 1 March 2010; Revised 4 June 2010; Accepted 2 August 2010 Academic Editor: Maria R. Baer Copyright © 2010 H. Ye and T. A. Rouault. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Erythropoiesis in animals is a synchronized process of erythroid cell differentiation that depends on successful acquisition of iron. Heme synthesis depends on iron through its dependence on iron sulfur (Fe-S) cluster biogenesis. Here, we review the relationship between Fe-S biogenesis and heme synthesis in erythropoiesis, with emphasis on the proteins, GLRX5, ABCB7, ISCA, and C1orf69. These Fe-S biosynthesis proteins are highly expressed in erythroid tissues, and deficiency of each of these proteins has been shown to cause anemia in zebrafish model. GLRX5 is involved in the production and ABCB7 in the export of an unknown factor that may function as a gauge of mitochondrial iron status, which may indirectly modulate activity of iron regulatory proteins (IRPs). ALAS2, the enzyme catalyzing the first step in heme synthesis, is translationally controlled by IRPs. GLRX5 may also provide Fe-S cofactor for ferrochelatase, the last enzyme in heme synthesis. ISCA and C1orf69 are thought t

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