Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1

Greene, Wayne K.; Baker, Elizabeth; Rabbitts, Terence H.; Kees, Ursula R.

doi:10.1016/s0378-1119(99)00125-0

Cited by 39 publications

(37 citation statements)

References 10 publications

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“…This is the first report that revealed the binding between FHL3 and NFY. FHL3 is a member of four-and-a-half LIM only protein (FHL) family including FHL1, FHL2, FHL3, FHL4, and ACT (25)(26)(27)(28)(29)(30). They only contain a single N-terminal half-LIM domain followed by four sequential LIM domains, belonging to a subset of the LIM protein superfamily which possesses cysteine-rich double zinc finger motifs called LIM.…”

Section: Discussionmentioning

confidence: 99%

Molecular Mechanisms for Transcriptional Regulation of Human High-Affinity IgE Receptor β-Chain Gene Induced by GM-CSF

Takahashi

Hayashi

Kaminogawa

et al. 2006

The Journal of Immunology

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The β-chain of the high-affinity receptor for IgE (FcεRI) plays an important role in regulating activation of FcεRI-expressing cells such as mast cells in allergic reactions. We already reported that the transcription factor myeloid zinc finger (MZF) 1 which formed a high m.w. complex including four and a half LIM-only protein (FHL)3 in the nucleus repressed human β-chain gene expression through an element in the fourth intron. We also found that GM-CSF induced expression of MZF-1 and nuclear translocation of FHL3. We screened a human cDNA library and identified NFY which was reported to bind histone deacetylases (HDACs) as a constituent of the complex. The C-subunit of NFY was demonstrated to form a ternary complex with MZF-1/FHL3 and interact with a β-chain gene region including the element in the fourth intron. HDAC1 and HDAC2 were also shown to interact with the fourth intron region of the β-chain gene. In a human mast cell line HMC-1 cultured with GM-CSF, both β-chain expression and acetylation of histones interacting with the fourth intron region of the β-chain gene were decreased. Collectively, these results indicated that HDACs, which were recruited to the β-chain gene through the element in the fourth intron by MZF-1/FHL3/NFY, repressed β-chain gene transcription by deacetylation of histones in the presence of GM-CSF. These mechanisms will be involved in not only the cell type-specific repression of β-chain gene expression in differentiating hemopoietic cells but also the repression of β-chain gene expression in the peripheral cells under specific circumstances.

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Section: Discussionmentioning

confidence: 99%

Molecular Mechanisms for Transcriptional Regulation of Human High-Affinity IgE Receptor β-Chain Gene Induced by GM-CSF

Takahashi

Hayashi

Kaminogawa

et al. 2006

The Journal of Immunology

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“…FHL proteins (FHL1, KyoT2, FHL2, FHL3, FHL4 and ACT) [15,16,18,[25][26][27] contain only a single N-terminal half-LIM domain followed by four sequential LIM domains, belonging to a subset of the LIM protein superfamily, which possesses cysteinerich double zinc finger motifs called LIM. No interaction between FHL1 and MZF-1 and poor interaction between FHL2 and MZF-1 were detected in the yeast two-hybrid assay (results not shown).…”

Section: Discussionmentioning

confidence: 99%

“…Human FHL1 and FHL2 cDNAs were obtained by RT (reverse transcriptase)-PCR and cloned into pCR3.1 to yield pCR3.1-FHL1 and pCR3.1-FHL2 respectively. The nucleotide sequences of synthetic oligonucleotides used as PCR primers are as follows [15,16]: FHL1, 5 -CATGGCGGAGAAGTTTGACTGCCAC-3 and 5 -GTTTACAGCTTTTTGGCACAGTCGG-3 ; FHL2, 5 -AA-TGACTGAGCGCTTTGACTGCCACC-3 and 5 -GTGTTGA-ATTCAGATGTCTTTCCCAC-3 .…”

Section: Experimental Plasmid Constructionmentioning

confidence: 99%

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FHL3 negatively regulates human high-affinity IgE receptor β-chain gene expression by acting as a transcriptional co-repressor of MZF-1

Takahashi

Matsumoto

2005

Biochemical Journal

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The high-affinity IgE receptor FcεRI plays a key role in triggering allergic reactions. We recently reported that human FcεRI β-chain gene expression was down-regulated by a transcription factor, MZF-1, through an element in the fourth intron. In the present study, we found that this transcriptional repression by MZF-1 required FHL3 (four and a half LIM domain protein 3) as a cofactor. Yeast two-hybrid and immunoprecipitation assays demonstrated that FHL3 bound MZF-1 in vitro and in vivo. Overexpression of FHL3 in KU812 cells suppressed the β-chain promoter activity through the element in the fourth intron in an MZF-1-dependent manner. Furthermore, results from pull-down assays and gel-filtration chromatography employing nuclear extracts indicated that MZF-1 and FHL3 formed a complex of high molecular mass with some additional proteins in the nucleus. Granulocyte-macrophage colony-stimulating factor, which was reported to decrease FcεRI expression, induced the accumulation of FHL3 in the nucleus, in accordance with the repressive role of FHL3 in β-chain gene expression.

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“…In mammals, this family consists of five members (ACT and FHL1-4) in which the characteristic property is a highly tissue-specific expression pattern. Although the expression of activator of cAMP-response element modulator (CREM) in testis (ACT) and FHL4 is restricted to testis (16,17,40), FHL1-3 are enriched in striated muscles (8,17,19,41,43) and involved in the regulation of cytoskeletal protein organization and transcription through their scaffolding and nuclear shuttling activities (6,9,44,52,59). We therefore further determined 1) whether FHL5 is colocalized with actin fibers in pillar cells, 2) whether it has a nuclear shuttling activity, and 3) whether its mRNA and protein levels undergo changes in response to tensions applied to pillar cells by volume expansion and treatment with ET-1, the receptor for which, and effects, have been documented in the gill lamellar vasculature (31,56,57).…”

mentioning

confidence: 99%

FHL5, a novel actin-binding protein, is highly expressed in eel gill pillar cells and responds to wall tension

Mistry

Kato²,

Tran³

et al. 2004

American Journal of Physiology-Regulatory, Integrative and Comp

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Supporting evidence for the contractile nature of fish branchial pillar cells was provided by demonstrating the presence of actin fibers and a novel four-and-a-half LIM (FHL) protein in which expression is specific for contractile tissues and sensitive to the tension applied to the pillar cell. When eel gill sections were stained with rhodamine-phalloidin, a selective fluorescent probe for fibrous actin, a strong bundle-like staining was observed around collagen columns in pillar cells, suggesting the presence of abundant actin fibers. A cDNA clone encoding a novel member of the actin-binding FHL family, FHL5, was isolated from a subtracted cDNA library of eel gill. Northern analysis revealed that FHL5 mRNA is highly expressed only in gills, heart, and skeletal muscle. In gills, FHL5 was found to be confined to pillar cells by immunohistochemistry. Confocal fluorescence microscopy showed that FHL5 is present in both cytosol and nucleus; within the cytosol, a large portion of FHL5 is colocalized with the phalloidin-positive actin bundles. Furthermore, transfection of myogenic C2C12 cells with FHL5 cDNA demonstrated, in addition to its interaction with actin stress fibers, a nuclear shuttling activity of FHL5. The mRNA and protein levels were found to be elevated on 1) transfer of eels from seawater to freshwater, 2) volume expansion by infusion of isotonic dextran-saline, and 3) constriction of gill vasculature by bolus injection of endothelin-1. These results suggest contractile nature of pillar cells and a role of FHL5 in maintaining the integrity and regulating the dynamics of pillar cells. C2C12 myoblast; endothelin; immunohistochemistry; lamella; zinc finger; four-and-a-half LIM FISH GILLS CONSIST OF a large number of filaments arranged along the gill arches. The surfaces of the filaments are greatly enlarged by a series of plate-like lamellae. Each lamella is composed of two sheets of epithelia separated by a thin space through which the blood circulates to allow the exchange of respiratory gases. The separation between the epithelial sheets is maintained by pillar cells and collagen bundles. Pillar cells are spool-shaped cells connecting two epithelial sheets of the respiratory lamella in fish gills (50,51,64). They are characterized by collagen bundles contained in the infoldings of the plasma membrane and are oriented perpendicularly to the epithelial sheets, which consist of a thin layer of pavement cells and a basal lamina that is continuous with the collagen bundles traversing the pillar cells (49, 64); for the anatomy of gill lamella, see the schematic illustration in Fig. 9D. The membrane-enclosed collagen bundles help prevent ballooning of the lamella. The inner surfaces of the two epithelial sheets are covered with flanges extended from the pillar cells, forming capillary lumen called lacunae. Another feature of the pillar cells is the presence of numerous myofilament-like structures that course through the cytoplasm in an orientation parallel to the collagen bundles. These myofilaments appear to ...

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Genomic structure, tissue expression and chromosomal location of the LIM-only gene, SLIM1

Cited by 39 publications

References 10 publications

Molecular Mechanisms for Transcriptional Regulation of Human High-Affinity IgE Receptor β-Chain Gene Induced by GM-CSF

Molecular Mechanisms for Transcriptional Regulation of Human High-Affinity IgE Receptor β-Chain Gene Induced by GM-CSF

FHL3 negatively regulates human high-affinity IgE receptor β-chain gene expression by acting as a transcriptional co-repressor of MZF-1

FHL5, a novel actin-binding protein, is highly expressed in eel gill pillar cells and responds to wall tension

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