Please use this identifier to cite or link to this item: https://doi.org/10.7554/eLife.01228
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dc.titleCytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization
dc.contributor.authorAraki, K.
dc.contributor.authorKawauchi, K.
dc.contributor.authorHirata, H.
dc.contributor.authorYamamoto, M.
dc.contributor.authorTaya, Y.
dc.date.accessioned2014-12-12T07:30:55Z
dc.date.available2014-12-12T07:30:55Z
dc.date.issued2013-12-03
dc.identifier.citationAraki, 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
dc.identifier.issn2050084X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/115662
dc.description.abstractSkeletal 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.7554/eLife.01228
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCANCER SCIENCE INSTITUTE OF SINGAPORE
dc.description.doi10.7554/eLife.01228
dc.description.sourcetitleeLife
dc.description.volume2013
dc.description.issue2
dc.description.page-
dc.identifier.isiut000328643800003
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