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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Online Access: | http://dx.doi.org/10.1155/2010/329394 |
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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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