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Regulation of Myosin Light Chain Function by BMP Signaling Controls Actin Cytoskeleton Remodeling
Department of Biochemistry, University of Crete Medical School, Heraklion, Greece.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm , Ludwig Institute for Cancer Research. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. Uppsala University, Science for Life Laboratory, SciLifeLab.
Department of Biochemistry, University of Crete Medical School, Heraklion, Greece.
2011 (English)In: Cellular Physiology and Biochemistry, ISSN 1015-8987, E-ISSN 1421-9778, Vol. 28, no 5, 1031-1044 p.Article in journal (Refereed) Published
Abstract [en]


Actin cytoskeleton dynamics support and coordinate signaling events that control cell proliferation, differentiation and migration. Growth factors provide essential signals that act on multi-protein complexes that regulate actin assembly with myosin. We previously analyzed the action of the transforming growth factor β (TGF-β) and now extend our studies to the bone morphogenetic protein (BMP) 7, an important regulator of stem cell function and bone differentiation.


Using a well-established cell model of actin dynamics, Swiss3T3 fibroblasts, we applied cell biological and biochemical approaches to monitor the pathway that links the BMP-7 receptors to the acto-myosin complex.


We demonstrate that BMP-7 induces actin and focal adhesion remodeling in starved fibroblasts as potently as TGF-β. BMP-7 mediates changes of actin dynamics via the kinase ROCK1 and induces rapid activation of RhoA and RhoB with concomitant inactivation of Cdc42. These molecular events correlate well with induction of phosphorylation on Ser19 of the myosin light chain, but not with LIMK1 kinase activation. Depletion of endogenous myosin light chain inhibits actin remodeling induced by BMP-7. This novel pathway regulates fibroblast migration without affecting cell proliferation.


We establish a BMP-Rho-ROCK1 pathway, which targets myosin light chain to control actin remodeling in fibroblasts.

Place, publisher, year, edition, pages
2011. Vol. 28, no 5, 1031-1044 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-166124DOI: 10.1159/000335790ISI: 000298488600023PubMedID: 22178953OAI: oai:DiVA.org:uu-166124DiVA: diva2:475321
Available from: 2012-01-10 Created: 2012-01-10 Last updated: 2012-04-03Bibliographically approved

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Moustakas, Aristidis
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Ludwig Institute for Cancer ResearchDepartment of Medical Biochemistry and MicrobiologyScience for Life Laboratory, SciLifeLab
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