Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0006155
Title: Cellular contractility requires ubiquitin mediated proteolysis
Authors: Cinnamon Y.
Feine O.
Hochegger H.
Bershadsky A. 
Brandeis M.
Keywords: myosin light chain
Rho kinase
ubiquitin
myosin light chain kinase
ubiquitin
animal cell
article
cell adhesion
cell function
controlled study
human
human cell
microtubule
nonhuman
protein degradation
protein function
protein phosphorylation
animal
cell line
hydrolysis
metabolism
phosphorylation
ubiquitination
Animals
Cell Line
Humans
Hydrolysis
Myosin-Light-Chain Kinase
Phosphorylation
Ubiquitin
Ubiquitination
Issue Date: 2009
Citation: Cinnamon Y., Feine O., Hochegger H., Bershadsky A., Brandeis M. (2009). Cellular contractility requires ubiquitin mediated proteolysis. PLoS ONE 4 (7) : e6155. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0006155
Abstract: Background: Cellular contractility, essential for cell movement and proliferation, is regulated by microtubules, RhoA and actomyosin. The RhoA dependent kinase ROCK ensures the phosphorylation of the regulatory Myosin II Light Chain (MLC) Ser19, thereby activating actomyosin contractions. Microtubules are upstream inhibitors of contractility and their depolymerization or depletion cause cells to contract by activating RhoA. How microtubule dynamics regulates RhoA remains, a major missing link in understanding contractility. Principal Findings: We observed that contractility is inhibited by microtubules not only, as previously reported, in adherent cells, but also in non-adhering interphase and mitotic cells. Strikingly we observed that contractility requires ubiquitin mediated proteolysis by a Cullin-RING ubiquitin ligase. Inhibition of proteolysis, ubiquitination and neddylation all led to complete cessation of contractility and considerably reduced MLC Ser19 phosphorylation. Conclusions: Our results imply that cells express a contractility inhibitor that is degraded by ubiquitin mediated proteolysis, either constitutively or in response to microtubule depolymerization. This degradation seems to depend on a Cullin-RING ubiquitin ligase and is required for cellular contractions. � 2009 Cinnamon et al.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161835
ISSN: 19326203
DOI: 10.1371/journal.pone.0006155
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