Journal of Cell Science

Journal: Journal of Cell Science

Abbreviation

J. Cell Sci.

Publisher

Company of Biologists

ISSN

1477-9137
0021-9533

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Publications 1 - 10 of 57

The bright and the dark sides of activin in wound healing and cancer
Antsiferova, Maria; Werner, Sabine (2012)
Journal of Cell Science
Increased keratinocyte proliferation by JUN-dependent expression of PTN and SDF-1 in fibroblasts
Florin, Lore; Maas-Szabowski, Nicole; Werner, Sabine; et al. (2005)
Journal of Cell Science
Keratinocyte growth factor protects epidermis and hair follicles from cell death induced by UV irradiation, chemotherapeutic or cytotoxic agents
Braun, Susanne; Krampert, Monika; Bodó, Enikö; et al. (2006)
Journal of Cell Science
Bartonella henselae engages inside-out and outside-in signaling by integrin β1 and talin1 during invasome-mediated bacterial uptake
Truttmann, Matthias C.; Misselwitz, Benjamin; Huser, Sonja; et al. (2011)
Journal of Cell Science
CRL4(RBBP7) is required for efficient CENP-A deposition at centromeres
Mouysset, Julien; Gilberto, Samuel; Meier, Michelle G.; et al. (2015)
Journal of Cell Science
A dual role of YAP in driving TGFβ-mediated endothelial-to-mesenchymal transition
Savorani, Cecillia; Malinverno, Matteo; Seccia, Roberta; et al. (2021)
Journal of Cell Science
Endothelial-to-mesenchymal transition (EndMT) is the biological process through which endothelial cells transdifferentiate into mesenchymal cells. During embryo development, EndMT regulates endocardial cushion formation via TGFβ/BMP signaling. In adults, EndMT is mainly activated during pathological conditions. Hence, it is necessary to characterize molecular regulators cooperating with TGFβ signaling in driving EndMT, to identify potential novel therapeutic targets to treat these pathologies. Here, we studied YAP, a transcriptional co-regulator involved in several biological processes, including epithelial-to-mesenchymal transition (EMT). As EndMT is the endothelial-specific form of EMT, and YAP (herein referring to YAP1) and TGFβ signaling cross-talk in other contexts, we hypothesized that YAP contributes to EndMT by modulating TGFβ signaling. We demonstrate that YAP is required to trigger TGFβ-induced EndMT response, specifically contributing to SMAD3-driven EndMT early gene transcription. We provide novel evidence that YAP acts as SMAD3 transcriptional co-factor and prevents GSK3β-mediated SMAD3 phosphorylation, thus protecting SMAD3 from degradation. YAP is therefore emerging as a possible candidate target to inhibit pathological TGFβ-induced EndMT at early stages.
BMP2 and FGF2 cooperate to induce neural-crest-like fates from fetal and adult CNS stem cells
Sailer, Martin H.M.; Hazel, Thomas G.; Panchision, David M.; et al. (2005)
Journal of Cell Science
Kinetochores accelerate centrosome separation to ensure faithful chromosome segregation
Mchedlishvili, Nunu; Wieser, Samuel; Holtackers, René; et al. (2012)
Journal of Cell Science
The IGFBP7 homolog Imp-L2 promotes insulin signaling in distinct neurons of the Drosophila brain
Bader, R.; Sarraf-Zadeh, L.; Peters, M.; et al. (2013)
Journal of Cell Science
Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway
Thomas, Franziska; Kutay, Ulrike (2003)
Journal of Cell Science
The production of ribosomes constitutes a major biosynthetic task for cells. Eukaryotic small and large ribosomal subunits are assembled in the nucleolus and independently exported to the cytoplasm. Most nuclear export pathways require RanGTP-binding export receptors. We analyzed the role of CRM1, the export receptor for leucine-rich nuclear export signals (NES), in the biogenesis of ribosomal subunits in vertebrate cells. Inhibition of the CRM1 export pathway led to a defect in nuclear export of both 40S and 60S subunits in HeLa cells. Moreover, the export of newly made ribosomal subunits in Xenopus oocytes was efficiently and specifically competed by BSA-NES conjugates. The CRM1 dependence of 60S subunit export suggested a conserved function for NMD3, a factor proposed to be a 60S subunit export adaptor in yeast. Indeed, we observed that nuclear export of human NMD3 (hNMD3) is sensitive to leptomycin B (LMB), which inactivates CRM1. It had, however, not yet been demonstrated that Nmd3 can interact with CRM1. Using purified recombinant proteins we have shown here that hNMD3 binds to CRM1 directly, in a RanGTP-dependent manner, by way of a C-terminal NES sequence. Our results suggest that the functions of CRM1 and NMD3 in ribosomal subunit export are conserved from yeast to higher eukaryotes. © The Company of Biologists Limited 2003.

Publications 1 - 10 of 57

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