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The RNA-binding protein Staufen1 impairs myogenic differentiation via a c-myc-dependent mechanism.

Ravel-Chapuis A, Crawford TE, Blais-Crépeau ML, Bélanger G, Richer CT, Jasmin BJ - Mol. Biol. Cell (2014)

Bottom Line: Cells overexpressing Staufen1 differentiated poorly, as evidenced by reductions in the differentiation and fusion indices and decreases in MyoD, myogenin, MEF2A, and MEF2C, independently of Staufen-mediated mRNA decay.By contrast, the knockdown of Staufen1 decreased c-myc levels in myoblasts.Collectively our results show that Staufen1 is highly expressed during early stages of differentiation/development and that it can impair differentiation by regulating c-myc, thereby highlighting the multifunctional role of Staufen1 in skeletal muscle cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.

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Staufen1 decreases during myogenic differentiation. (A, B) Western blots showing Staufen1 and myogenin protein levels in differentiating SkMCs and HSMM, respectively. β-Actin was used as a loading control. (C) Representative Western blots showing Staufen1 and myogenin protein levels in differentiating C2C12 cells. β-Actin was used to show equal loading. (D) Relative quantification of Staufen1 and myogenin protein levels from differentiating C2C12 cells, respectively (n = 3). Asterisks indicate significance (*p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001).
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Figure 3: Staufen1 decreases during myogenic differentiation. (A, B) Western blots showing Staufen1 and myogenin protein levels in differentiating SkMCs and HSMM, respectively. β-Actin was used as a loading control. (C) Representative Western blots showing Staufen1 and myogenin protein levels in differentiating C2C12 cells. β-Actin was used to show equal loading. (D) Relative quantification of Staufen1 and myogenin protein levels from differentiating C2C12 cells, respectively (n = 3). Asterisks indicate significance (*p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001).

Mentions: Primary human skeletal muscle cells (SkMCs) and myoblasts (HSMM) isolated from normal donors were also used to assess expression of Staufen1 during myogenic differentiation. The switch from high to low serum culture conditions induces myoblasts to exit the cell cycle and initiates differentiation by promoting the fusion of primary myoblasts into elongated, multinucleated myotubes. We thus measured the level of Staufen1 protein expression by Western blot during human primary cell differentiation and observed a progressive decrease in Staufen1 levels as cells differentiate (Figure 3, A and B). In fact, Staufen1 levels steadily decreased within 1–4 d after the switch to low serum, a time corresponding to the engagement of cells into the differentiation process, as confirmed by the induction of myogenin (Figure 3A).


The RNA-binding protein Staufen1 impairs myogenic differentiation via a c-myc-dependent mechanism.

Ravel-Chapuis A, Crawford TE, Blais-Crépeau ML, Bélanger G, Richer CT, Jasmin BJ - Mol. Biol. Cell (2014)

Staufen1 decreases during myogenic differentiation. (A, B) Western blots showing Staufen1 and myogenin protein levels in differentiating SkMCs and HSMM, respectively. β-Actin was used as a loading control. (C) Representative Western blots showing Staufen1 and myogenin protein levels in differentiating C2C12 cells. β-Actin was used to show equal loading. (D) Relative quantification of Staufen1 and myogenin protein levels from differentiating C2C12 cells, respectively (n = 3). Asterisks indicate significance (*p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4230783&req=5

Figure 3: Staufen1 decreases during myogenic differentiation. (A, B) Western blots showing Staufen1 and myogenin protein levels in differentiating SkMCs and HSMM, respectively. β-Actin was used as a loading control. (C) Representative Western blots showing Staufen1 and myogenin protein levels in differentiating C2C12 cells. β-Actin was used to show equal loading. (D) Relative quantification of Staufen1 and myogenin protein levels from differentiating C2C12 cells, respectively (n = 3). Asterisks indicate significance (*p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001).
Mentions: Primary human skeletal muscle cells (SkMCs) and myoblasts (HSMM) isolated from normal donors were also used to assess expression of Staufen1 during myogenic differentiation. The switch from high to low serum culture conditions induces myoblasts to exit the cell cycle and initiates differentiation by promoting the fusion of primary myoblasts into elongated, multinucleated myotubes. We thus measured the level of Staufen1 protein expression by Western blot during human primary cell differentiation and observed a progressive decrease in Staufen1 levels as cells differentiate (Figure 3, A and B). In fact, Staufen1 levels steadily decreased within 1–4 d after the switch to low serum, a time corresponding to the engagement of cells into the differentiation process, as confirmed by the induction of myogenin (Figure 3A).

Bottom Line: Cells overexpressing Staufen1 differentiated poorly, as evidenced by reductions in the differentiation and fusion indices and decreases in MyoD, myogenin, MEF2A, and MEF2C, independently of Staufen-mediated mRNA decay.By contrast, the knockdown of Staufen1 decreased c-myc levels in myoblasts.Collectively our results show that Staufen1 is highly expressed during early stages of differentiation/development and that it can impair differentiation by regulating c-myc, thereby highlighting the multifunctional role of Staufen1 in skeletal muscle cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.

Show MeSH
Related in: MedlinePlus