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Id sustains Hes1 expression to inhibit precocious neurogenesis by releasing negative autoregulation of Hes1.
Results indicate that Id proteins participate in NSC maintenance through sustaining Hes1 expression in early embryos through interacting directly with Hes1 and releasing the negative feedback autoregulation of Hes1 without interfering with its ability to affect other target genes. Expand
Vascular endothelial hyperpermeability induces the clinical symptoms of Clarkson disease (the systemic capillary leak syndrome).
A model of SCLS pathogenesis in which nonimmunoglobulin humoral factors such as VEGF and Ang2 contribute to transient endothelial contraction is supported, suggesting a molecular mechanism for this highly lethal disorder. Expand
Intranuclear Actin Regulates Osteogenesis
Increased intranuclear actin forces MSC into osteogenic lineage through controlling Runx2 activity; this process may be useful for clinical objectives of forming bone. Expand
Mechanical strain inhibits adipogenesis in mesenchymal stem cells by stimulating a durable beta-catenin signal.
The results indicate that MSC commitment to adipogenesis can be suppressed by mechanical signals, allowing other signals to promote osteoblastogenesis, and suggest that positive effects of exercise on both fat and bone may occur during mesenchymal lineage selection. Expand
β-Catenin Levels Influence Rapid Mechanical Responses in Osteoblasts*
- N. Case, Meiyun Ma, B. Sen, Z. Xie, T. Gross, J. Rubin
- Biology, Medicine
- Journal of Biological Chemistry
- 24 October 2008
Mechanical strain activates Akt and inactivates GSK3β to allow β-catenin translocation, and Wnt signaling through LRP5 is not required for these strain-mediated responses, which serves as both a modulator and effector of mechanical signals in bone cells. Expand
Mechanical Regulation of Glycogen Synthase Kinase 3β (GSK3β) in Mesenchymal Stem Cells Is Dependent on Akt Protein Serine 473 Phosphorylation via mTORC2 Protein*
- N. Case, Jacob Thomas, +4 authors J. Rubin
- Biology, Medicine
- The Journal of Biological Chemistry
- 28 September 2011
In sum, mechanical input initiates a signaling cascade that is uniquely dependent on mTORC2 activation and phosphorylation of Akt at Ser-473, an effect sufficient to cause inactivation of GSK3β. Expand
R4 RGS proteins: regulation of G-protein signaling and beyond.
This review highlights recent advances in the understanding of the physiological functions of one subfamily of RGS proteins with a high degree of homology (B/R4) gleaned from recent studies of knockout mice or cells with reduced RGS expression. Expand
Retinoic acid regulates bone morphogenic protein signal duration by promoting the degradation of phosphorylated Smad1
- Nengyin Sheng, Z. Xie, +8 authors N. Jing
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 18 October 2010
The results reveal a mechanism by which RA suppresses BMP signaling through regulation of pSmad1 stability, and this cross-talk between RA and BMP pathways is involved in the proper patterning of dorsal neural tube of chicken embryo. Expand
mTORC2 Regulates Mechanically Induced Cytoskeletal Reorganization and Lineage Selection in Marrow‐Derived Mesenchymal Stem Cells
- B. Sen, Z. Xie, +4 authors J. Rubin
- Medicine, Biology
- Journal of bone and mineral research : the…
- 1 January 2014
The data show that mTORC2 is involved in stem cell responses to biophysical stimuli, regulating both signaling and cytoskeletal reorganization, preventing adipogenesis by preserving β‐catenin and stimulating osteogenesis by generating a stiffer cytoskeleton. Expand
Cell Mechanosensitivity to Extremely Low‐Magnitude Signals Is Enabled by a LINCed Nucleus
It is shown that MSC response to LMS is enabled through mechanical coupling between the cytoskeleton and the nucleus, in turn activating FAK and Akt signaling followed by FAK‐dependent induction of RhoA, indicating that the MSC responds to its dynamic physical environment not only with “outside‐in’ signaling initiated by substrate strain, but vibratory signals enacted through the LINC complex enable matrix independent “inside–inside” signaling. Expand