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Title: Force interacts with macromolecular structure in activation of TGF-β

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Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nature (London); Journal Volume: 542; Journal Issue: 7639
Country of Publication:
United States

Citation Formats

Dong, Xianchi, Zhao, Bo, Iacob, Roxana E., Zhu, Jianghai, Koksal, Adem C., Lu, Chafen, Engen, John R., and Springer, Timothy A. Force interacts with macromolecular structure in activation of TGF-β. United States: N. p., 2017. Web. doi:10.1038/nature21035.
Dong, Xianchi, Zhao, Bo, Iacob, Roxana E., Zhu, Jianghai, Koksal, Adem C., Lu, Chafen, Engen, John R., & Springer, Timothy A. Force interacts with macromolecular structure in activation of TGF-β. United States. doi:10.1038/nature21035.
Dong, Xianchi, Zhao, Bo, Iacob, Roxana E., Zhu, Jianghai, Koksal, Adem C., Lu, Chafen, Engen, John R., and Springer, Timothy A. Wed . "Force interacts with macromolecular structure in activation of TGF-β". United States. doi:10.1038/nature21035.
title = {Force interacts with macromolecular structure in activation of TGF-β},
author = {Dong, Xianchi and Zhao, Bo and Iacob, Roxana E. and Zhu, Jianghai and Koksal, Adem C. and Lu, Chafen and Engen, John R. and Springer, Timothy A.},
abstractNote = {},
doi = {10.1038/nature21035},
journal = {Nature (London)},
number = 7639,
volume = 542,
place = {United States},
year = {Wed Jan 25 00:00:00 EST 2017},
month = {Wed Jan 25 00:00:00 EST 2017}
  • Heat-shock cognate protein 70 (Hsc70), a molecular chaperone constitutively expressed in the cell, is involved in the regulation of several cellular signaling pathways. In this study, we found that TGF-β-induced phosphorylation and nuclear translocation of Smad2/3 were suppressed in fibroblastic NRK-49F cells treated with small interfering RNA (siRNA) for Hsc70. In the cells underexpressing Hsc70, transcriptional induction of connective tissue growth factor (CTGF), a target gene of the TGF-β signaling, was also suppressed in the early phase of TGF-β stimulation. Upon stimulation with TGF-β, Hsc70 interacted with Smad2/3, suggesting functional interactions of Hsc70 and Smad2/3 for the activation of TGF-β-inducedmore » Smad signaling. Although the expression of heat-shock protein 70 (Hsp70) was upregulated in the cells treated with Hsc70 siRNA, TGF-β-induced Smad activation was not affected in the cells overexpressing Hsp70. Collectively, these results indicate that Hsc70, but not Hsp70, supportively regulates TGF-β-induced Smad signaling in NRK-49F cells. - Highlights: • Hsc70 siRNA treatment suppressed the expression of Hsc70 but induced the expression of Hsp70 in NRK-49F cells. • Hsc70 siRNA treatment suppressed the activation of Smad2/3 in the cells treated with TGF-β. • Hsc70 interacted with Smad2/3 on stimulation with TGF-β in the cells. • Hsp70 did not influence the TGF-β-induced activation of Smad2/3 in the cells overexpressing Hsp70.« less
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  • No abstract prepared.
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