Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart

Chan, Kwok Keung; Tsui, Stephen Kwok‐Wing; Lee, Simon Ming‐Yuen; Luk, Sharon; Liew, Choong Chin; Fung, Kwok‐Pui; Waye, Mary Miu Yee; Lee, Cheuk Yu

doi:10.1016/s0378-1119(97)00644-6

Cited by 123 publications

(110 citation statements)

References 40 publications

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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%

“…After RT reaction using 1 µg of the total RNA as a template and an oligo(dT) [12][13][14][15][16][17][18] primer (Invitrogen), PCR was performed with two primer sets. Nucleotide sequences of the primers used for the PCR are as follows.…”

Section: Rt-pcrmentioning

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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Section: Discussionmentioning

confidence: 99%

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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“…Although expression of FHL2 is predominantly detected in the heart (Chan et al, 1998), it has also been observed in several extracardiac tissues at certain stages of development and in many (if not all) different cell lines in culture, including U2OS (Amaar et al, 2002) and fibroblastic cells used in this work. In these cell lines, FHL2 has been reported to localize in several cellular compartments, including focal adhesions (Scholl et al, 2000;Li et al, 2001;Gabriel et al, 2004), cytoplasm and nucleus (Scholl et al, 2000;Muller et al, 2002;Morlon and Sassone-Corsi, 2003).…”

Section: Lim-only Protein Fhl2 Is a Negative Regulator Of E4f1mentioning

confidence: 91%

“…DARL/FHL2 is strongly expressed in cardiac and skeletal muscle cells and, at lower levels, in many other tissues, cell types and established cell lines (Chan et al, 1998;Chu et al, 2000a, b;Scholl et al, 2000;Tanahashi and Tabira, 2000;Kong et al, 2001;Muller et al, 2002;Gabriel et al, 2004;Kang et al, 2003). It encodes a member of the FHL protein family (FHL1-4, ACT), a subclass of the LIM-only protein family, that contains four and an half copies of the cysteine-rich LIM motif (CX2CX16-23HX2CX2CX2CX16-21CX2-3(C/H/D), a widely represented protein domain which functions as an adapter or modifier in protein interactions (Retaux and Bachy, 2002).…”

Section: Introductionmentioning

confidence: 99%

The LIM-only protein FHL2 is a negative regulator of E4F1

et al. 2006

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The E1A-targeted transcription factor E4F1 is a key player in the control of mammalian embryonic and somatic cell proliferation and survival. Mouse embryos lacking E4F die at an early developmental stage, whereas enforced expression of E4F1 in various cell lines inhibits cell cycle progression. E4F1-antiproliferative effects have been shown to depend on its capacity to repress transcription and to interact with pRb and p53. Here we show that full-length E4F1 protein (p120 E4F1 ) but not its E1A-activated and truncated form (p50 E4F1 ), interacts directly in vitro and in vivo with the LIM-only protein FHL2, the product of the p53-responsive gene FHL2/ DRAL (downregulated in rhabdomyosarcoma Lim protein). This E4F1-FHL2 association occurs in the nuclear compartment and inhibits the capacity of E4F1 to block cell proliferation. Consistent with this effect, ectopic expression of FHL2 inhibits E4F1 repressive effects on transcription and correlates with a reduction of nuclear E4F1-p53 complexes. Overall, these results suggest that FHL2/DRAL is an inhibitor of E4F1 activity. Finally, we show that endogenous E4F1-FHL2 complexes form in U2OS cells upon UV-light-induced nuclear accumulation of FHL2.

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Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1)

et al. 1999

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We characterized a human cDNA clone encoding a 36-kDa carboxyl terminal LIM domain protein with a PDZ domain at the amino terminal. This full-length cDNA clone has a predicted open reading frame (ORF) of 329 amino-acid residues. The ORF of this cDNA encodes the human homolog of rat CLP36, and the putative protein is named human 36-kDa carboxyl terminal LIM domain protein (hCLIM1, nomenclature approved by the HUGO/GDB Nomenclature Committee). The hCLIM1 probe was used to hybridize with poly(A)+ RNA of various human tissues. Strong signals were detected in heart and skeletal muscle; moderate signals were detected in spleen, small intestine, colon, placenta, and lung; weaker levels were detected in liver, thymus, kidney, prostate, and pancreas; and no observable signals were detected in brain, testis, ovary, and peripheral blood leukocytes. The hCLIM1 gene was studied by fluorescence in situ hybridization (FISH), somatic cell hybrid analysis, and radiation hybrid mapping, and it is located at the human chromosome 10q26.

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Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart

Cited by 123 publications

References 40 publications

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

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

The LIM-only protein FHL2 is a negative regulator of E4F1

Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1)

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