Nuclear Function of Smad7 Promotes Myogenesis

@article{Miyake2009NuclearFO,
  title={Nuclear Function of Smad7 Promotes Myogenesis},
  author={Tetsuaki Miyake and Nezeka S. Alli and John C. McDermott},
  journal={Molecular and Cellular Biology},
  year={2009},
  volume={30},
  pages={722 - 735},
  url={https://api.semanticscholar.org/CorpusID:38662598}
}
Smad7 has a nuclear coactivator function that is independent of TGF-β signaling and necessary to promote myogenic differentiation and Reporter and myogenic conversion assays indicate a pivotal regulation of MyoD transcriptional properties by the balance between Smad7 and active MEK.

Maintenance of the Undifferentiated State in Myogenic Progenitor Cells by TGFβ Signaling is Smad Independent and Requires MEK Activation

Observations support a model in which TGFβ activates a MEK/ERK/c-Jun pathway to repress skeletal myogenesis, maintaining the pluripotent undifferentiated state in myogenic progenitors.

Smad7:β-catenin complex regulates myogenic gene transcription

These studies document a novel function of a Smad7-MED12/13-β-catenin complex at the ckm locus, indicating a key role of this complex in the program of myogenic gene expression underlying skeletal muscle development and regeneration.

Regulation of TGF-β Family Signaling by Inhibitory Smads.

The vertebrate I-Smads, their roles as inhibitors of Smad activation and regulators of receptor stability, as scaffolds for non-Smad signaling, and their possible roles in the nucleus are discussed.

The Dual Role of Smad7 in the Control of Cancer Growth and Metastasis

Data emerging from experimental studies indicate that Smad7 may differently modulate the course of various tumors depending on the context analyzed, and suggest that therapeutic interventions around Smad 7 can help interfere with the development/progression of human cancers.

Nuclear Smad7 Overexpressed in Mesenchymal Cells Acts as a Transcriptional Corepressor by Interacting with HDAC-1 and E2F to Regulate Cell Cycle

The present results strongly suggest that nuclear Smad7 is a transcriptional corepressor for E2F, providing a molecular basis for the Smad 7-induced arrest of the cell cycle.

Transforming Growth Factor-β Signaling

Members of the transforming growth factor β (TGF-β) family regulate cell proliferation, migration, and differentiation during embryonal development and in tissue homeostasis in the adult. They signal

Krüppel-like factor 6 (KLF6) promotes cell proliferation in skeletal myoblasts in response to TGFβ/Smad3 signaling

KLF6 and MEF2D are co-localized in the nuclei of mononucleated but not multinucleated myogenic cells and, that theMEF2 cis element is a key component of the KLF6 promoter region, implicate KLF 6 in myoblast proliferation and survival in response to TGFβ.

Linc-smad7 promotes myoblast differentiation and muscle regeneration via sponging miR-125b

Results of RNA immunoprecipitation analysis and biotin-labeled miR-125b capture suggest that Linc-smad7 could act as a competing endogenous RNA (ceRNA) for miRNA- 125b, and suggest that the novel noncoding regulator Lincoln-smAD7 regulates skeletal muscle development.

Role of a SET/Smad7 Interaction in Skeletal Myogenesis

It is suggested that the manuscript should be rewritten in a chapters-by- chapters format to facilitate more detailed discussion of the author's research and its findings.

Smad7 Promotes and Enhances Skeletal Muscle Differentiation

Data implicate Smad7 as a fundamental regulator of differentiation in skeletal muscle cells as well as the muscle regulatory factor (MyoD), which binds to and transactivates the Smad 7 proximal promoter region and enhances MyoD transcriptional activity.

Transforming growth factor beta1 induces nuclear export of inhibitory Smad7.

It is reported that Smad7, but not Smad6, inhibits TGF-beta1-induced growth inhibition and the expression of immediate early response genes, including Smad 7, which suggests a functional role distinct from its antagonistic effect in receptor-mediated Smad activation.

Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling.

The identification of Smad7 is reported, which is related to Smad6 and associates stably with the TGF-beta receptor complex, but is not phosphorylated upon TGF -beta stimulation.

Identification of Smad7, a TGFβ-inducible antagonist of TGF-β signalling

The identification of Smad7 is reported, which is related to Smad6 and associates stably with the TGF-β receptor complex, but is not phosphorylated upon T GF-β stimulation.

The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling.

A novel function for MAD-related proteins as intracellular antagonists of the type I kinase domain of TGFbeta family receptors is defined as blocking the association, phosphorylation, and activation of Smad2.

Direct binding of Smad3 and Smad4 to critical TGFβ‐inducible elements in the promoter of human plasminogen activator inhibitor‐type 1 gene

The identification of Smad3/Smad4 binding sequences, termed CAGA boxes, within the promoter of the human PAI‐1 gene is reported, which suggest that this may be a widely used motif in TGFβ‐regulated transcription.

Inhibition of transforming growth factor-β/SMAD signalling by the interferon-γ/STAT pathway

The results indicate a mechanism of transmodulation between the STAT and SMAD signal-transduction pathways that prevents the interaction of Smad3 with the TGF-β receptor.

Smad4 Dependency Defines Two Classes of Transforming Growth Factor β (TGF-β) Target Genes and Distinguishes TGF-β-Induced Epithelial-Mesenchymal Transition from Its Antiproliferative and Migratory Responses

Results suggest that loss of Smad4 might promote TGF-β-mediated tumorigenesis by abolishing tumor-suppressive functions of T GF-β while maintaining some tumor-promoting TGF -β responses.
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