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The transcription factor <t>MAFA</t> targets the GHR gene to promote muscle growth. a Venn diagram showing the overlap between MAFA target genes identified by ChIP-seq and differentially expressed genes from transcriptome analysis. b ChIP-seq peak profile indicating binding of MAFA to the GHR gene. c Heatmap showing Pearson correlation coefficients among expression levels of GHR and MAFA (FPKM values) and the proportion of longissimus dorsi muscle (n = 10). d Western blot analysis validating the <t>chromatin</t> <t>immunoprecipitation</t> (ChIP) efficiency of MAFA. Input: Cell lysate after centrifugation; SN: Supernatant after immunoprecipitation; IP: Antibody-magnetic bead complex after incubation and washing; IgG: IgG-magnetic bead complex after incubation and washing. e ChIP-PCR results showing significant enrichment of the GHR gene by MAFA (n = 3). f – h Western blot analysis of GHR expression and JAK2 phosphorylation levels in the longissimus dorsi muscle of individuals with different genotypes (n = 3, same batch of samples as in Fig. e, with shared β-actin internal control). Data are presented as mean ± SEM. Statistical significance is indicated as follows: ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.005; **** P < 0.001; ***** P < 0.0005
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The transcription factor <t>MAFA</t> targets the GHR gene to promote muscle growth. a Venn diagram showing the overlap between MAFA target genes identified by ChIP-seq and differentially expressed genes from transcriptome analysis. b ChIP-seq peak profile indicating binding of MAFA to the GHR gene. c Heatmap showing Pearson correlation coefficients among expression levels of GHR and MAFA (FPKM values) and the proportion of longissimus dorsi muscle (n = 10). d Western blot analysis validating the <t>chromatin</t> <t>immunoprecipitation</t> (ChIP) efficiency of MAFA. Input: Cell lysate after centrifugation; SN: Supernatant after immunoprecipitation; IP: Antibody-magnetic bead complex after incubation and washing; IgG: IgG-magnetic bead complex after incubation and washing. e ChIP-PCR results showing significant enrichment of the GHR gene by MAFA (n = 3). f – h Western blot analysis of GHR expression and JAK2 phosphorylation levels in the longissimus dorsi muscle of individuals with different genotypes (n = 3, same batch of samples as in Fig. e, with shared β-actin internal control). Data are presented as mean ± SEM. Statistical significance is indicated as follows: ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.005; **** P < 0.001; ***** P < 0.0005
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The transcription factor <t>MAFA</t> targets the GHR gene to promote muscle growth. a Venn diagram showing the overlap between MAFA target genes identified by ChIP-seq and differentially expressed genes from transcriptome analysis. b ChIP-seq peak profile indicating binding of MAFA to the GHR gene. c Heatmap showing Pearson correlation coefficients among expression levels of GHR and MAFA (FPKM values) and the proportion of longissimus dorsi muscle (n = 10). d Western blot analysis validating the <t>chromatin</t> <t>immunoprecipitation</t> (ChIP) efficiency of MAFA. Input: Cell lysate after centrifugation; SN: Supernatant after immunoprecipitation; IP: Antibody-magnetic bead complex after incubation and washing; IgG: IgG-magnetic bead complex after incubation and washing. e ChIP-PCR results showing significant enrichment of the GHR gene by MAFA (n = 3). f – h Western blot analysis of GHR expression and JAK2 phosphorylation levels in the longissimus dorsi muscle of individuals with different genotypes (n = 3, same batch of samples as in Fig. e, with shared β-actin internal control). Data are presented as mean ± SEM. Statistical significance is indicated as follows: ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.005; **** P < 0.001; ***** P < 0.0005
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The transcription factor <t>MAFA</t> targets the GHR gene to promote muscle growth. a Venn diagram showing the overlap between MAFA target genes identified by ChIP-seq and differentially expressed genes from transcriptome analysis. b ChIP-seq peak profile indicating binding of MAFA to the GHR gene. c Heatmap showing Pearson correlation coefficients among expression levels of GHR and MAFA (FPKM values) and the proportion of longissimus dorsi muscle (n = 10). d Western blot analysis validating the <t>chromatin</t> <t>immunoprecipitation</t> (ChIP) efficiency of MAFA. Input: Cell lysate after centrifugation; SN: Supernatant after immunoprecipitation; IP: Antibody-magnetic bead complex after incubation and washing; IgG: IgG-magnetic bead complex after incubation and washing. e ChIP-PCR results showing significant enrichment of the GHR gene by MAFA (n = 3). f – h Western blot analysis of GHR expression and JAK2 phosphorylation levels in the longissimus dorsi muscle of individuals with different genotypes (n = 3, same batch of samples as in Fig. e, with shared β-actin internal control). Data are presented as mean ± SEM. Statistical significance is indicated as follows: ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.005; **** P < 0.001; ***** P < 0.0005
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The transcription factor MAFA targets the GHR gene to promote muscle growth. a Venn diagram showing the overlap between MAFA target genes identified by ChIP-seq and differentially expressed genes from transcriptome analysis. b ChIP-seq peak profile indicating binding of MAFA to the GHR gene. c Heatmap showing Pearson correlation coefficients among expression levels of GHR and MAFA (FPKM values) and the proportion of longissimus dorsi muscle (n = 10). d Western blot analysis validating the chromatin immunoprecipitation (ChIP) efficiency of MAFA. Input: Cell lysate after centrifugation; SN: Supernatant after immunoprecipitation; IP: Antibody-magnetic bead complex after incubation and washing; IgG: IgG-magnetic bead complex after incubation and washing. e ChIP-PCR results showing significant enrichment of the GHR gene by MAFA (n = 3). f – h Western blot analysis of GHR expression and JAK2 phosphorylation levels in the longissimus dorsi muscle of individuals with different genotypes (n = 3, same batch of samples as in Fig. e, with shared β-actin internal control). Data are presented as mean ± SEM. Statistical significance is indicated as follows: ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.005; **** P < 0.001; ***** P < 0.0005

Journal: Genetics, Selection, Evolution : GSE

Article Title: A 3′ UTR polymorphism g.1618 G > A in the MAFA gene modulates miR-3678-3p binding and enhances meat production in sheep via the MAFA/GHR/JAK2 pathway

doi: 10.1186/s12711-025-01024-7

Figure Lengend Snippet: The transcription factor MAFA targets the GHR gene to promote muscle growth. a Venn diagram showing the overlap between MAFA target genes identified by ChIP-seq and differentially expressed genes from transcriptome analysis. b ChIP-seq peak profile indicating binding of MAFA to the GHR gene. c Heatmap showing Pearson correlation coefficients among expression levels of GHR and MAFA (FPKM values) and the proportion of longissimus dorsi muscle (n = 10). d Western blot analysis validating the chromatin immunoprecipitation (ChIP) efficiency of MAFA. Input: Cell lysate after centrifugation; SN: Supernatant after immunoprecipitation; IP: Antibody-magnetic bead complex after incubation and washing; IgG: IgG-magnetic bead complex after incubation and washing. e ChIP-PCR results showing significant enrichment of the GHR gene by MAFA (n = 3). f – h Western blot analysis of GHR expression and JAK2 phosphorylation levels in the longissimus dorsi muscle of individuals with different genotypes (n = 3, same batch of samples as in Fig. e, with shared β-actin internal control). Data are presented as mean ± SEM. Statistical significance is indicated as follows: ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.005; **** P < 0.001; ***** P < 0.0005

Article Snippet: Immunoprecipitation was performed using an anti-MAFA antibody (#79,737, Cell Signaling Technology, USA), and IgG served as a negative control.

Techniques: ChIP-sequencing, Binding Assay, Expressing, Western Blot, Chromatin Immunoprecipitation, Centrifugation, Immunoprecipitation, Incubation, Phospho-proteomics, Control