The Differentiation of Skeletal Muscle Cells Involves a Protein-tyrosine Phosphatase-α-mediated C-Src Signaling Pathway

Lu, Huogen; Shah, Poonam; Ennis, David; Shinder, Gail; Sap, Jan; Le-Tien, Hoang; Fantus, I. George

doi:10.1074/jbc.m209643200

Cited by 30 publications

(26 citation statements)

References 65 publications

(87 reference statements)

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“…A physiological role of Src in myogenesis is suggested by a previous report showing that it is activated in differentiating L6 myoblasts, and that its inhibition prevents myogenin expression and myotube formation (Lu et al, 2002). By contrast, overexpression of v-Src, a constitutively active oncogenic mutant of Src, in myoblasts inhibits myoblast differentiation (Falcone et al, 1991;Falcone et al, 2003;Yoon and Boettiger, 1994).…”

Section: Discussionmentioning

confidence: 97%

Src mediates the mechanical activation of myogenesis by activating TNFα-converting enzyme

Niu

Wen

Liu

et al. 2013

Journal of Cell Science

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SummaryMechanical stimulation affects many biological aspects in living cells through mechanotransduction. In myogenic precursor cells (MPCs), mechanical stimulation activates p38 mitogen-activated protein kinase (MAPK), a key regulator of myogenesis, via activating TNFa-converting enzyme (TACE, also known as ADAM17), to release autocrine TNFa. However, the signaling mechanism of mechanical activation of TACE is unknown. Because TACE possesses the structural features of substrates of the non-receptor tyrosine kinase Src, we tested the hypothesis that Src mediates mechanical activation of TACE in MPCs. We observed that mechanical stretch of C2C12 or primary rat myoblasts rapidly activates Src, which in turn interacts and colocalizes with TACE, resulting in tyrosine phosphorylation and activation of TACE. Particularly, Src activates TACE via the phosphorylation of amino acid residue Tyr702 in the intracellular tail of TACE, resulting in increased TNFa release and p38 activation. Src inhibition or deficiency blocks stretch activation of the TACE-p38-MAPK signaling, resulting in impaired myogenic gene expression. In response to functional overloading, Src and TACE are activated in mouse soleus muscle. Further, overloading-induced myogenesis and regeneration are impaired in the soleus of Src +/2 mice. Therefore, Src mediates mechano-activation of TACE and myogenesis.

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Section: Discussionmentioning

confidence: 97%

Src mediates the mechanical activation of myogenesis by activating TNFα-converting enzyme

Niu

Wen

Liu

et al. 2013

Journal of Cell Science

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“…Furthermore, to move our body parts efficiently, our locomotive organs, that is, musculoskeletal systems, are required to respond to changes in motion and forces. Humans and animals therefore possess the molecular machinery for mechanosensing and mechanotransduction, and these include Src and p130Cas, both of which are involved in the normal differentiation of muscle 81,99 as well as bone cells 100,101 (Fig. 3A).…”

Section: Mechanical Regulation Of Src and P130cas Is Distinguished Bementioning

confidence: 99%

Src, p130Cas, and Mechanotransduction in Cancer Cells

2012

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Anchorage-independent growth is the most significant hallmark of cell transformation, which has an intimate relevance to cancer. Anchorage or adhesion physically links cells to the extracellular matrix and allows the transmission of external mechanical cues to intracellular signaling machineries. Transformation involves acquiring the ability to proliferate without requiring mechanically initiated signal transduction, known as mechanotransduction. A number of signaling and cytoskeletal molecules are located at focal adhesions. Src and its related proteins, including p130Cas, localize to adhesion sites, where their functions can be mechanically regulated. In addition, the aberrant activation and expression of Src and p130Cas are linked to transformation and malignancy both in vitro and in vivo. These findings shed light on the importance of mechanotransduction in tumorigenesis and the regulation of cancer progression and also provide insights into the mechanical aspects of cancer signaling.

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“…C-Src is not only important for mitogen signal transduction, but also is known to be essential for muscle fiber differentiation (Lu et al 2002). Dephosphorylation of c-Src kinase leads to an accelerated differentiation seemingly by an activation of p38 mitogen-activated protein kinase (MAPK), which enhances the transcriptional activities of MyoD and myocyte enhancer binding factor2 (Lu et al 2002;Lim et al 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Dephosphorylation of c-Src kinase leads to an accelerated differentiation seemingly by an activation of p38 mitogen-activated protein kinase (MAPK), which enhances the transcriptional activities of MyoD and myocyte enhancer binding factor2 (Lu et al 2002;Lim et al 2007). …”

Section: Discussionmentioning

confidence: 99%

Differentiation-dependent PTPIP51 Expression in Human Skeletal Muscle Cell Culture

Barop

Sauer

Steger

et al. 2009

J Histochem Cytochem.

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S U M M A R Y Protein tyrosine phosphatase-interacting protein 51 (PTPIP51) expression was analyzed in proliferating and differentiating human myogenic cells cultured in vitro. Satellite cell cultures derived from four different individuals were used in this study. To analyze the expression of PTPIP51, myoblasts were cultured under conditions promoting either proliferation or differentiation. In addition, further differentiation of already-differentiated myobtubes was inhibited by resubmitting the cells to conditions promoting proliferation. PTPIP51 protein and mRNA were investigated in samples taken at defined time intervals by immunostaining, immunoblotting, in situ hybridization, and PCR. Image analyses of fluorescence immunostainings were used to quantify PTPIP51 in cultured myoblasts and myotubes. Myoblasts grown in the presence of epidermal and fibroblast growth factors (EGF and FGF), both promoting proliferation, expressed PTPIP51 on a basic level. Differentiation to multinuclear myotubes displayed a linear increase in PTPIP51 expression. The rise in PTPIP51 protein was paralleled by an augmented expression of muscle-specific proteins, namely, sarcoplasmic reticulum Ca 21 ATPase and myosin heavy-chain protein, both linked to a progressive state of myotubal differentiation. This differentiation-induced increase in PTPIP51 was partly reversible by resubmission of differentiated myotubes to conditions boosting proliferation. The results clearly point toward a strong association between PTPIP51 expression and differentiation in human muscle cells. (J Histochem Cytochem 57:425-435, 2009)

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The Differentiation of Skeletal Muscle Cells Involves a Protein-tyrosine Phosphatase-α-mediated C-Src Signaling Pathway

Cited by 30 publications

References 65 publications

Src mediates the mechanical activation of myogenesis by activating TNFα-converting enzyme

Src mediates the mechanical activation of myogenesis by activating TNFα-converting enzyme

Src, p130Cas, and Mechanotransduction in Cancer Cells

Differentiation-dependent PTPIP51 Expression in Human Skeletal Muscle Cell Culture

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