NDLI: Control of myofibroblast differentiation by microtubule dynamics through a regulated localization of mDia2.

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Control of myofibroblast differentiation by microtubule dynamics through a regulated localization of mDia2.

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Control of myofibroblast differentiation by microtubule dynamics through a regulated localization of mDia2.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dulin, Nickolai Kach, Jacob Sandbo, Nathan Kregel, Steve Ngam, Caitlyn Torr, Elizabeth
Description	Author Affiliation: Sandbo N ( Division of Allergy, Pulmonary, and Critical Care, University of Wisconsin, Madison, Wisconsin 53792, USA. nsandbo@medicine.wisc.edu)
Abstract	Myofibroblast differentiation plays a critical role in wound healing and in the pathogenesis of fibrosis. We have previously shown that myofibroblast differentiation is mediated by the activity of serum response factor (SRF), which is tightly controlled by the actin polymerization state. In this study, we investigated the role of the microtubule cytoskeleton in modulating myofibroblast phenotype. Treatment of human lung fibroblasts with the microtubule-destabilizing agent, colchicine, resulted in a formation of numerous stress fibers and expression of myofibroblast differentiation marker proteins. These effects of colchicine were independent of Smad signaling but were mediated by Rho signaling and SRF, as they were attenuated by the Rho kinase inhibitor, Y27632, or by the SRF inhibitor, CCG-1423. TGF-ß-induced myofibroblast differentiation was not accompanied by gross changes in the microtubule polymerization state. However, microtubule stabilization by paclitaxel attenuated TGF-ß-induced myofibroblast differentiation. Paclitaxel had no effect on TGF-ß-induced Smad activation and Smad-dependent gene transcription but inhibited actin polymerization, nuclear accumulation of megakaryoblastic leukemia-1 protein, and SRF activation. The microtubule-associated formin, mDIA2, localized to actin stress fibers upon treatment with TGF-ß, and paclitaxel prevented this localization. Treatment with the formin inhibitor, SMI formin homology 2 domain, inhibited stress fiber formation and myofibroblast differentiation induced by TGF-ß, without affecting Smad-phosphorylation or microtubule polymerization. Together, these data suggest that (a) TGF-ß promotes association of mDia2 with actin stress fibers, which further drives stress fiber formation and myofibroblast differentiation, and (b) microtubule polymerization state controls myofibroblast differentiation through the regulation of mDia2 localization.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	22
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-05-31
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adaptor Proteins, Signal Transducing Metabolism Cell Differentiation Physiology Microtubule-Associated Proteins Microtubules Myofibroblasts Amides Pharmacology Anilides Benzamides Drug Effects Cells, Cultured Colchicine DNA-Binding Proteins Enzyme Inhibitors Gene Expression Regulation Cytology Oncogene Proteins, Fusion Paclitaxel Protein Transport Pyridines Serum Response Factor Smad Proteins Genetics Stress Fibers Trans-Activators Transforming Growth Factor Beta Tubulin Modulators Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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