Association of erythroid transcription factors: complexes involving the LIM protein RBTN2 and the zinc-finger protein GATA1.

Osada, H; Grütz, Gerald; Axelson, Håkan; Förster, A.; Rabbitts, Terence H.

doi:10.1073/pnas.92.21.9585

Cited by 181 publications

(155 citation statements)

References 35 publications

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“…It was first identified by its ability to bind functionally important DNA regulatory sequences found in globin genes [43,44]. Several proteins have been reported to interact physically with GATA-1, including EKLF/Sp1 [45], LMO-2 [46], FOG-1 [47], p300/ CBP [48], and PU.1 [49][50][51]. We did not find any association between GATA-1 expression and BP1 inhibition in K562 cells.…”

Section: Discussionmentioning

confidence: 36%

Inhibition of β protein 1 expression enhances β-globin promoter activity and β-globin mRNA levels in the human erythroleukemia (K562) cell line

Zoueva¹,

Rodgers²

2004

Experimental Hematology

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Expression of globin genes within the β-globin cluster is regulated to produce different hemoglobin β chains during the embryonic (ε), fetal (γ), and adult (β) stages of erythroid cell development. Each distinct hemoglobin tetramer exhibits a different affinity for oxygen, resulting in optimal O 2 / CO 2 exchange between the developing fetus and mother. Thus, developmentally appropriate transcriptional activation of each different β chain is essential. This is achieved by the binding of transcriptional activator proteins to the successive β-chain promoters; the locus control region (LCR), consisting of five DNase I-hypersensitive sites (HS1-5) located from 8 to 22 kbp 5′ to the ε-globin gene, also Offprint requests to:

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Section: Discussionmentioning

confidence: 36%

Inhibition of β protein 1 expression enhances β-globin promoter activity and β-globin mRNA levels in the human erythroleukemia (K562) cell line

Zoueva¹,

Rodgers²

2004

Experimental Hematology

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“…One possibility, based on studies of LMO-1 and -2 in the hematopoietic system, is that LMO-4 recruits Clim-2 to DNA gene regulatory complexes that contain GET-1. In erythroid cells, LMO-2 interacts with the E-box binding TAL1/SCL-E12 heterodimer (Begley et al, 1989;Chen et al, 1990) and with GATA factors (Osada et al, 1995;Wadman et al, 1997). These experiments (Valge-Archer et al, 1994;Wadman et al, 1994Wadman et al, , 1997Osada et al, 1995;Larson et al, 1996;Visvader et al, 1997) and work in Xenopus embryos (Bao et al, 2000) suggest a model in which LMO factors can tether to DNA by associating with DNA binding proteins, thus allowing the coregulator Clims to interact with transactivators that do not contain covalently linked LIM domains.…”

Section: Discussionmentioning

confidence: 98%

“…Although LMOs are transcriptional regulators that do not associate directly with DNA (Bach, 2000), work with LMO-2 in erythroid cells suggests that LMOs may act by interacting with DNA-binding proteins (Osada et al, 1995;Visvader et al, 1997;Wadman et al, 1997). Therefore, we decided to search for LMO-4 -interacting DNA-binding proteins in epidermis.…”

Section: Cloning Of Get-1 From Mouse Epidermismentioning

confidence: 99%

Identification and characterization of Grainyhead‐like epithelial transactivator (GET‐1), a novel mammalian Grainyhead‐like factor

Kudryavtseva¹,

Sugihara²,

Wang³

et al. 2003

Developmental Dynamics

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LMO-4 is an LIM-only factor that is highly expressed in many epithelial cells, including those of the epidermis and hair follicles. Because LMOs may function by interacting with DNA-binding proteins, we have used the yeast two-hybrid system to screen mouse skin libraries for LMO-4 -interacting DNA-binding proteins. In this screen, we isolated a novel LMO-4 -interacting factor highly related to the Drosophila gene Grainyhead. Grainyhead is epidermally expressed and carries out important functions in cuticular formation in the fly embryo. With the identification of this novel mammalian Grainyhead-like gene, referred to as Grainyhead-like epithelial transactivator 1 (GET-1), the known members of the mammalian Grainyhead-like gene family are extended to six, falling into two classes based on sequence homology. Of interest, the expression pattern of GET-1 is similar to that of Drosophila Grainyhead with highest expression in the somatic ectoderm/epidermis, but GET-1 is additionally expressed in epithelial cells of gastrointestinal, genitourinary, and respiratory tracks. The GET-1 protein localizes to the nucleus and binds to at least one Grainyhead DNA-binding site. The GET-1 DNA-binding domain maps to a region containing homology to the Drosophila Grainyhead DNA-binding domain. GET-1 homodimerizes in solution by means of a short C-terminally located domain that is homologous to other Grainyhead-like genes. A short domain located between amino acids 100 and 190, which bears no homology to known transactivation domains, is sufficient to confer transactivation to the heterologous GAL4 DNA-binding domain. In addition, GET-1 appears to contain repression domains consistent with the observation that Grainyhead and other mammalian Grainyhead-like genes can act both as activators and repressors. These data suggest that GET-1 is a transcriptional regulator that may perform important functions in epithelial tissues of mammals. Developmental Dynamics 226:604 -617, 2003.

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“…11 In both its normal and leukemogenic roles LMO2 protein is thought to act as a transcription regulator, both because it is located in the nucleus 7 and because it forms complexes with the transcription factors RBP-2, tal-1, GATA-1, and GATA-2. [12][13][14] We have also identified a novel transcription factor, ELF2, belonging to the ets family of transcription factors, that associates with LMO2 and may play a role in leukemogenesis. 15 Additionally, we have recently demonstrated that LMO2 is a complex transcription factor, possessing multiple transcription regulatory modules, including two activation domains and two repression domains.…”

Section: Introductionmentioning

confidence: 99%

Identification of genes potentially involved in LMO2-induced leukemogenesis

2000

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The most common translocations in childhood T cell acute lymphoblastic leukemias involve the LMO2 locus on chromosome 11p13 and cause ectopic expression of the LMO2 gene in thymocytes. Transgenic mice with enforced expression of LMO2 in their thymocytes develop T cell leukemias thus demonstrating the role of LMO2 in leukemogenesis. The physiologic and leukemogenic functions of LMO2 are mediated through its transcriptional regulatory activities, but the identity of the target genes is completely unknown. In this report, we have used cDNA representational difference analysis (cDNA-RDA) to identify genes that are over-expressed and are likely to play a role in the LMO2 induced leukemias. cDNA-RDA was performed using very small amounts of mRNA pool (from 1 g of total RNA) to reverse transcribe the cDNAs from leukemic cells or normal thymocytes. The cDNA-RDA led to the isolation of nine distinct clones that were specifically overexpressed in the leukemic cells. Sequence analysis revealed that five of the nine clones had identity or homology to known genes that are known to play a role in the pathogenesis of leukemias or other cancers. Three clones had no significant homology to any known genes and thus represent novel candidate genes. Our study demonstrates that cDNA-RDA using very small amounts of total RNA is a highly efficient method to identify novel genes that may play a role in leukemogenesis.

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Association of erythroid transcription factors: complexes involving the LIM protein RBTN2 and the zinc-finger protein GATA1.

Cited by 181 publications

References 35 publications

Inhibition of β protein 1 expression enhances β-globin promoter activity and β-globin mRNA levels in the human erythroleukemia (K562) cell line

Inhibition of β protein 1 expression enhances β-globin promoter activity and β-globin mRNA levels in the human erythroleukemia (K562) cell line

Identification and characterization of Grainyhead‐like epithelial transactivator (GET‐1), a novel mammalian Grainyhead‐like factor

Identification of genes potentially involved in LMO2-induced leukemogenesis

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