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|Title:||Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization||Authors:||Araki, K.
|Issue Date:||3-Dec-2013||Citation:||Araki, K., Kawauchi, K., Hirata, H., Yamamoto, M., Taya, Y. (2013-12-03). Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization. eLife 2013 (2) : -. ScholarBank@NUS Repository. https://doi.org/10.7554/eLife.01228||Abstract:||Skeletal muscle degeneration is a complication arising from a variety of chronic diseases including advanced cancer. Pro-inflammatory cytokine TNF-α plays a pivotal role in mediating cancer-related skeletal muscle degeneration. Here, we show a novel function for retinoblastoma protein (Rb), where Rb causes sarcomeric disorganization. In human skeletal muscle myotubes (HSMMs), up-regulation of cyclin-dependent kinase 4 (CDK4) and concomitant phosphorylation of Rb was induced by TNF-α treatment, resulting in the translocation of phosphorylated Rb to the cytoplasm. Moreover, induced expression of the nuclear exporting signal (NES)-fused form of Rb caused disruption of sarcomeric organization. We identified mammalian diaphanous-related formin 1 (mDia1), a potent actin nucleation factor, as a binding partner of cytoplasmic Rb and found that mDia1 helps maintain the structural integrity of the sarcomere. These results reveal a novel non-nuclear function for Rb and suggest a potential mechanism of TNF-α-induced disruption of sarcomeric organization. © Araki et al.||Source Title:||eLife||URI:||http://scholarbank.nus.edu.sg/handle/10635/115662||ISSN:||2050084X||DOI:||10.7554/eLife.01228|
|Appears in Collections:||Staff Publications|
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