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Wnt/β-catenin signaling for dental regeneration

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Yang Z., Liu F.
Stem Cells in Oral Medicine
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2012
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vol. 1
3-8
EN
Emerging regenerative strategies are promising to cure the irreversible damages to dental tissues, but the success of these strategies is constrained by the lack of insight on the molecular cues of regeneration, while recent advancements on the molecular controls of development of dental tissues provided valuable clues for identifying potential regenerative cues. Wnt/β-catenin signaling pathway is highly conserved in animals and regulates the differentiation, proliferation, death and function of many cell and tissue types. This pathway is essential for morphogenesis and homeostasis of multiple oral organs, including teeth, taste buds, salivary glands and oral mucosa. Following injury, this pathway is activated in salivary glands and teeth, which contributes to repair or regeneration of damaged tissues. Consistently, activation of the Wnt/β-catenin signaling pathway in mice prevents radiation-induced damages or promotes regeneration of these dental tissues. In this review we discuss our current understanding and potential application of Wnt/β-catenin signaling in dental regeneration.
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PDZ domain from Dishevelled - a specificity study

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Śmietana K., Mateja A., Krężel A., Otlewski J.
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2011
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vol. 58
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issue 2
243-250
EN
Intracellular signaling cascades induced by Wnt proteins play a key role in developmental processes and are implicated in cancerogenesis. It is still unclear how the cell determines which of the three possible Wnt response mechanisms should be activated, but the decision process is most likely dependent on Dishevelled proteins. Dishevelled family members interact with many diverse targets, however, molecular mechanisms underlying these binding events have not been comprehensively described so far. Here, we investigated the specificity of the PDZ domain from human Dishevelled-2 using C-terminal phage display, which led us to identification of a leucine-rich binding motif strongly resembling the consensus sequence of a nuclear export signal. PDZ interactions with several peptide and protein motifs (including the nuclear export signal sequence from Dishevelled-2 protein) were investigated in detail using fluorescence spectroscopy, mutational analysis and immunoenzymatic assays. The experiments showed that the PDZ domain can bind the nuclear export signal sequence of the Dishevelled-2 protein. Since the intracellular localization of Dishevelled is governed by nuclear localization and nuclear export signal sequences, it is possible that the intramolecular interaction between PDZ domain and the export signal could modulate the balance between nuclear and cytoplasmic pool of the Dishevelled protein. Such a regulatory mechanism would be of utmost importance for the differential activation of Wnt signaling cascades, leading to selective promotion of the nucleus-dependent Wnt β-catenin pathway at the expense of non-canonical Wnt signaling.
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