The mammalian target of rapamycin signaling pathway regulates myocyte enhancer factor‐2C phosphorylation levels through integrin‐linked kinase in goat skeletal muscle satellite cells

Wang, Haiqing; Ren, Yu; Pan, Wei; Dong, Zhenguo; Cang, Ming; Liu, Dongjun

doi:10.1002/cbin.10499

Cited by 6 publications

(5 citation statements)

References 33 publications

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“…Despite considerable interest, it remains unclear how mTOR signals to establish early steps of myogenic commitment in muscle stem cells. Multiple genetic studies and our data in Figure 4E suggest the requirement of the Raptor-containing mTOR complex 1 (mTORC1), but not the Rictor-containing mTORC2 to mediate the early steps of myogenic commitment (Bentzinger et al, 2008;Hung et al, 2014;Rodgers et al, 2014;Wan et al, 2006;Wu et al, 2015). One of the major substrates of mTORC1, p70S6K1 is dispensable for the early steps of the myogenesis program ( Figure 4E and (Ge and Chen, 2012;Ohanna et al, 2005)).…”

Section: Discussionmentioning

confidence: 91%

mTORC1 activates PASK-Wdr5 signaling to epigenetically connect the nutrient status with myogenesis

Kikani

Fogarty

et al. 2017

Preprint

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SummaryIn the tissue microenvironment, stem cell functions are modulated by extrinsic signaling cues such as peptide hormones and dietary nutrients. These signaling cues maintain the balance between self-renewal and differentiation of its resident stem cells. The mechanistic Target of Rapamycin Complex 1 (mTORC1) is implicated to play an important role in regulating this balance, although its downstream effectors in stem cells have been elusive. We have recently shown that the PASK protein kinase phosphorylates Wdr5 to stimulate muscle stem cell differentiation by epigenetically activating the Myogenin promoter. Here, we show that the PASK-Wdr5 signaling pathway is a nutrient-sensitive downstream target of mTORC1 in muscle stem cells. We show that phosphorylation of PASK, and in turn of Wdr5, by mTORC1 is required for the activation of Myogenin transcription, exit from the self-renewal and induction of the myogenesis program. Thus, mTOR connects the diverse extrinsic signaling cues to a central epigenetic process to regulate the muscle stem cell fate between self-renewal and differentiation.

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Section: Discussionmentioning

confidence: 91%

mTORC1 activates PASK-Wdr5 signaling to epigenetically connect the nutrient status with myogenesis

Kikani

Fogarty

et al. 2017

Preprint

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“…The unique protein structure enables ILK to play an important role in the coordination of extracellular matrix (ECM) and the signal transduction of growth factor [ 28 , 29 ]. Evidence suggests that ILK may directly phosphorylate proteins associated with tumorigenesis by increasing cell proliferation, enhancing anchor independence of growth factors, and inhibition of apoptosis [ 14 , 30 , 31 ]. Investigations also revealed that MEF2C phosphorylation level increased significantly after ILK inhibition and knocking down, and the MCK expression that plays a vital role in the proliferation and differentiation of muscle cells increased significantly, suggesting that MEF2C transcription increased significantly after ILK inhibition or knocking down.…”

Section: Discussionmentioning

confidence: 99%

“…ILK regulates the phosphorylation of Akt at Ser473 and of glycogen synthase kinase 3 (GSK3) in various cell types [ 13 ]. We found that ILK also directly regulates MEF2C phosphorylation in the skeletal muscle cells of goats [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

Activated Integrin-Linked Kinase Negatively Regulates Muscle Cell Enhancement Factor 2C in C2C12 Cells

Dong

Pan

Wang

et al. 2015

BioMed Research International

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Our previous study reported that muscle cell enhancement factor 2C (MEF2C) was fully activated after inhibition of the phosphorylation activity of integrin-linked kinase (ILK) in the skeletal muscle cells of goats. It enhanced the binding of promoter or enhancer of transcription factor related to proliferation of muscle cells and then regulated the expression of these genes. In the present investigation, we explored whether ILK activation depended on PI3K to regulate the phosphorylation and transcriptional activity of MEF2C during C2C12 cell proliferation. We inhibited PI3K activity in C2C12 with LY294002 and then found that ILK phosphorylation levels and MEF2C phosphorylation were decreased and that MCK mRNA expression was suppressed significantly. After inhibiting ILK phosphorylation activity with Cpd22 and ILK-shRNA, we found MEF2C phosphorylation activity and MCK mRNA expression were increased extremely significantly. In the presence of Cpd22, PI3K activity inhibition increased MEF2C phosphorylation and MCK mRNA expression indistinctively. We conclude that ILK negatively and independently of PI3K regulated MEF2C phosphorylation activity and MCK mRNA expression in C2C12 cells. The results provide new ideas for the study of classical signaling pathway of PI3K-ILK-related proteins and transcription factors.

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“…Briefly, samples containing 1-3 mg total protein were precleared with Protein A/G Sepharose for 30 min. The cleared lysates were incubated with 4 mg anti-Tβ4 at 4 • C for at least 2 h, and up to overnight [37].…”

Section: Co-immunoprecipitation (Co-ip)mentioning

confidence: 99%

The Overexpression of Tβ4 in the Hair Follicle Tissue of Alpas Cashmere Goats Increases Cashmere Yield and Promotes Hair Follicle Development

Dai

Liang

Guo

et al. 2019

Animals

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Increased cashmere yield and improved quality are some goals of cashmere goat breeding. Thymosin beta-4 (Tβ4) plays a key role in the growth and development of hair follicles. For the past ten years, we have evaluated the role of Tβ4 by establishing a flock of 15 cashmere goats that specifically overexpress the Tβ4 gene in the hair follicles. These Tβ4 overexpression (Tβ4-OE) cashmere goats had more secondary hair follicles than the WT goats and produced more cashmere. Meanwhile, combined analysis of the skin transcriptome and proteome in cashmere goats suggested that Tβ4 may affect hair growth by interacting with keratin type II cytoskeletal 4 epidermal (KRT4) to mediate the extracellular signal-regulated protein kinase (ERK) signaling pathway, thereby promoting the development of secondary hair follicles, and consequently, increasing cashmere yield. Thus, the specific overexpression of Tβ4 in the hair follicles of cashmere goats effectively increased the cashmere yield.

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The mammalian target of rapamycin signaling pathway regulates myocyte enhancer factor‐2C phosphorylation levels through integrin‐linked kinase in goat skeletal muscle satellite cells

Cited by 6 publications

References 33 publications

mTORC1 activates PASK-Wdr5 signaling to epigenetically connect the nutrient status with myogenesis

mTORC1 activates PASK-Wdr5 signaling to epigenetically connect the nutrient status with myogenesis

Activated Integrin-Linked Kinase Negatively Regulates Muscle Cell Enhancement Factor 2C in C2C12 Cells

The Overexpression of Tβ4 in the Hair Follicle Tissue of Alpas Cashmere Goats Increases Cashmere Yield and Promotes Hair Follicle Development

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