Erythropoiesis and Iron Sulfur Cluster Biogenesis

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 synt...

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Main Authors: Hong Ye, Tracey A. Rouault
Format: Article
Language:English
Published: Hindawi Limited 2010-01-01
Series:Advances in Hematology
Online Access:http://dx.doi.org/10.1155/2010/329394
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spelling doaj-e3a7fb384d324862b71dd4460d7496112021-07-02T10:57:23ZengHindawi LimitedAdvances in Hematology1687-91041687-91122010-01-01201010.1155/2010/329394329394Erythropoiesis and Iron Sulfur Cluster BiogenesisHong Ye0Tracey A. Rouault1Molecular Medicine Program, Eunice Kennedy Shriver National Institutes of Child Health and Human Development at (NIH), 9000 Rockville Pike, Bethesda, MD 20892, USAMolecular Medicine Program, Eunice Kennedy Shriver National Institutes of Child Health and Human Development at (NIH), 9000 Rockville Pike, Bethesda, MD 20892, USAErythropoiesis 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 to assemble Fe-S clusters for mitochondrial aconitase and for lipoate synthase, the enzyme producing lipoate for pyruvate dehydrogenase complex (PDC). PDC and aconitase are involved in the production of succinyl-CoA, a substrate for heme biosynthesis. Thus, many steps of heme synthesis depend on Fe-S cluster assembly.http://dx.doi.org/10.1155/2010/329394
collection DOAJ
language English
format Article
sources DOAJ
author Hong Ye
Tracey A. Rouault
spellingShingle Hong Ye
Tracey A. Rouault
Erythropoiesis and Iron Sulfur Cluster Biogenesis
Advances in Hematology
author_facet Hong Ye
Tracey A. Rouault
author_sort Hong Ye
title Erythropoiesis and Iron Sulfur Cluster Biogenesis
title_short Erythropoiesis and Iron Sulfur Cluster Biogenesis
title_full Erythropoiesis and Iron Sulfur Cluster Biogenesis
title_fullStr Erythropoiesis and Iron Sulfur Cluster Biogenesis
title_full_unstemmed Erythropoiesis and Iron Sulfur Cluster Biogenesis
title_sort erythropoiesis and iron sulfur cluster biogenesis
publisher Hindawi Limited
series Advances in Hematology
issn 1687-9104
1687-9112
publishDate 2010-01-01
description 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 to assemble Fe-S clusters for mitochondrial aconitase and for lipoate synthase, the enzyme producing lipoate for pyruvate dehydrogenase complex (PDC). PDC and aconitase are involved in the production of succinyl-CoA, a substrate for heme biosynthesis. Thus, many steps of heme synthesis depend on Fe-S cluster assembly.
url http://dx.doi.org/10.1155/2010/329394
work_keys_str_mv AT hongye erythropoiesisandironsulfurclusterbiogenesis
AT traceyarouault erythropoiesisandironsulfurclusterbiogenesis
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