MEKK1-dependent phosphorylation of calponin-3 tunes cell contractility

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MEKK1-dependent phosphorylation of calponin-3 tunes cell contractility
Title:
MEKK1-dependent phosphorylation of calponin-3 tunes cell contractility
Journal Title:
Journal of Cell Science
Publication Date:
01 October 2016
Citation:
Journal of Cell Science (2016) 129, 3574-3582 doi:10.1242/jcs.189415
Abstract:
MEKK1 (also known as MAP3K1), which plays a major role in MAPK signaling, has been implicated in mechanical processes in cells, such as migration. Here, we identify the actin-binding protein calponin-3 as a new MEKK1 substrate in the signaling that regulates actomyosin-based cellular contractility. MEKK1 colocalizes with calponin-3 at the actin cytoskeleton and phosphorylates it, leading to an increase in the cell-generated traction stress. MEKK1-mediated calponin-3 phosphorylation is attenuated by the inhibition of myosin II activity, the disruption of actin cytoskeletal integrity and adhesion to soft extracellular substrates, whereas it is enhanced upon cell stretching. Our results reveal the importance of the MEKK1-calponin-3 signaling pathway to cell contractility.
License type:
PublisherCopyrights
Funding Info:
This work was supported by the National Research Foundation Singapore, under its Research Centre of Excellence, the Mechanobiology Institute.
Description:
The full paper is available for download at the publishers URL: https://doi.org/10.1242/jcs.189415
ISSN:
0021-9533
1477-9137
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