The mouse muscle creatine kinase promoter faithfully drives reporter gene expression in transgenic<i>Xenopus laevis</i>

Lim, Wayland; Neff, Eric S.; Furlow, J. David

doi:10.1152/physiolgenomics.00148.2003

Cited by 14 publications

(7 citation statements)

References 43 publications

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“…Yet as shown here, a rat MRF4 0.4-kb proximal promoter is at least minimally effective in transgenic Xenopus , demonstrating an important functional difference between the two transgenic systems. This conclusion differs from previous studies of mammalian promoters in transgenic X. laevis (e.g., Beck and Slack, 1999; Lim et al ., 2004) which emphasized the similarities of transgene expression in the two systems. In those studies, however, proximal promoters that lacked activity in mice were not tested in for activity Xenopus .…”

Section: Discussioncontrasting

confidence: 99%

A conserved MRF4 promoter drives transgenic expression in Xenopus embryonic somites and adult muscle

Hinterberger

2010

Int. J. Dev. Biol.

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The muscle regulatory factor MRF4 is expressed in both embryonic and adult vertebrate skeletal muscle cells. In mammals the MRF4 gene has a complex cis-regulatory structure, with many kilobases (kb) of upstream sequence required for embryonic expression in transgenic mice. Here, initial functional comparison between Xenopus and mammalian MRF4 genes revealed that 610 base pairs (bp) of the XMRF4a proximal promoter drove substantial transgenic expression in X. laevis myogenic cells, from somites of neurula embryos through adult myofibers, and as little as 180 bp gave detectable expression. Over 300 bp of XMRF4a proximal promoter sequence is highly conserved among three X. laevis and X. tropicalis MRF4 genes, but only about 150 bp shows significant identity to mammalian MRF4 genes. This most-conserved XMRF4a region contains a putative MEF2 binding site essential for expression both in transgenic embryos and in transfected mouse muscle cells. A rat MRF4 minimal promoter including the conserved region also was active in transgenic X. laevis embryos, demonstrating a striking difference between the mouse and Xenopus transgenic systems. The longest XMRF4a promoter construct tested, with 9.5 kb of 5′-flanking sequence, produced significantly greater expression in transfected mouse cells than did promoters 4.3-kb or shorter, suggesting that the intervening region contains an enhancer, although no increased expression was evident when this region was included in transgenic X. laevis embryos. Further identification and analysis of Xenopus MRF4 transcriptional control elements will offer insights into the evolution of this gene and of the myogenic gene regulatory network.

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Section: Discussioncontrasting

confidence: 99%

A conserved MRF4 promoter drives transgenic expression in Xenopus embryonic somites and adult muscle

Hinterberger

2010

Int. J. Dev. Biol.

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“…The transcript levels of MyoD and of muscle-specific genes such as muscle creatine kinase (17) were also further increased by co-transfection of Epc1 and SRF (Fig. 3, C and D).…”

Section: Epc1mentioning

confidence: 81%

Enhancer of Polycomb1 Acts on Serum Response Factor to Regulate Skeletal Muscle Differentiation

Kim

Kee

Kim

et al. 2009

Journal of Biological Chemistry

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Skeletal muscle differentiation is well regulated by a series of transcription factors. We reported previously that enhancer of polycomb1 (Epc1), a chromatin protein, can modulate skeletal muscle differentiation, although the mechanisms of this action have yet to be defined. Here we report that Epc1 recruits both serum response factor (SRF) and p300 to induce skeletal muscle differentiation. Epc1 interacted physically with SRF. Transfection of Epc1 to myoblast cells potentiated the SRF-induced expression of skeletal muscle-specific genes as well as multinucleation. Proximal CArG box in the skeletal ␣-actin promoter was responsible for the synergistic activation of the promoter-luciferase. Epc1 knockdown caused a decrease in the acetylation of histones associated with serum response element (SRE) of the skeletal ␣-actin promoter. The Epc1⅐SRF complex bound to the SRE, and the knockdown of Epc1 resulted in a decrease in SRF binding to the skeletal ␣-actin promoter. Epc1 recruited histone acetyltransferase activity, which was potentiated by cotransfection with p300 but abolished by si-p300. Epc1 directly bound to p300 in myoblast cells. Epc1 ؉/؊ mice showed distortion of skeletal ␣-actin, and the isolated myoblasts from the mice had impaired muscle differentiation. These results suggest that Epc1 is required for skeletal muscle differentiation by recruiting both SRF and p300 to the SRE of muscle-specific gene promoters.

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“…More specifically, the SOCS-3 gene was ligated out of the pEF plasmid using XbaI and subsequently cloned into the XbaI site of the previously described MCK-green fluorescent protein (GFP) plasmid (23). Using an inverse PCR strategy, primers were generated to allow for removal of the stop codon after the GFP sequence, which allowed for the creation of a N-terminal SOCS-3 GFP fusion construct.…”

Section: Mck-socs-3-gfp Constructmentioning

confidence: 99%

SOCS-3 Induces Myoblast Differentiation

Spangenburg

2005

Journal of Biological Chemistry

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Myoblast differentiation is characterized by a sequence of events that includes an increase in insulinlike growth factor (IGF)-I and contractile gene expression. The increase in IGF-I expression activates cell signaling mechanisms that participate in the differentiation process. One potential contributor is the SOCS-3 (suppressor of cytokine signaling-3) gene, which regulates signaling mechanisms and may be sensitive to changes in IGF-I concentrations. For the first time, the role of SOCS-3 is investigated in myoblast differentiation. SOCS-3 mRNA levels and SOCS-3 transcriptional activity increase during myoblast differentiation. SOCS-3 gene expression is induced, at least in part, by activation of the IGF-I receptor during myoblast differentiation. Overexpression of SOCS-3 cDNA significantly increased transcriptional activation of the 2.0-kb skeletal ␣-actin promoter in differentiating C2C12 myoblasts. In addition, overexpression of SOCS-3 specifically increased serum response factor-driven transcriptional activity but had no effect on nuclear-factor of activated T cell-driven transcriptional activity. SOCS-3 overexpression induced skeletal ␣-actin transcription in a myoblast cell line that cannot respond to endogenous IGF-I, indicating that SOCS-3 can contribute to the myoblast differentiation process in the absence of IGF-I. These data suggest that IGF-I induces myoblast differentiation, in part, by increasing SOCS-3 expression.

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The mouse muscle creatine kinase promoter faithfully drives reporter gene expression in transgenicXenopus laevis

Cited by 14 publications

References 43 publications

A conserved MRF4 promoter drives transgenic expression in Xenopus embryonic somites and adult muscle

A conserved MRF4 promoter drives transgenic expression in Xenopus embryonic somites and adult muscle

Enhancer of Polycomb1 Acts on Serum Response Factor to Regulate Skeletal Muscle Differentiation

SOCS-3 Induces Myoblast Differentiation

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