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First published online 11 November 2008
doi: 10.1242/jcs.031286

Journal of Cell Science 121, 3960-3970 (2008)
Published by The Company of Biologists 2008
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Research Article

BMP2 induction of actin cytoskeleton reorganization and cell migration requires PI3-kinase and Cdc42 activity

Cristina Gamell1,*, Nelson Osses1,2,*, Ramon Bartrons1, Thomas Rückle3, Montserrat Camps3, José Luis Rosa1 and Francesc Ventura1,{ddagger}

1 Departament de Ciències Fisiològiques II, Universitat de Barcelona, IDIBELL, L'Hospitalet de Llobregat, Spain
2 Instituto de Química, Facultad de Ciencias, Pontificia Universidad Católica de Valparaíso, Chile
3 Departments of Chemistry and Signal Transduction, Merck Serono SA, Research Center Geneva, 9, chemin des Mines, 1211 Geneva, Switzerland

{ddagger} Author for correspondence (e-mail: fventura{at}ub.edu)

Accepted 5 September 2008

Bone morphogenetic proteins (BMPs) are potent regulators of several cellular events. We report that exposure of C2C12 cells to BMP2 leads to an increase in cell migration and a rapid rearrangement of the actin filaments into cortical protrusions. These effects required independent and parallel activation of the Cdc42 small GTPase and the {alpha}-isoform of the phosphoinositide 3-kinase (PI3K{alpha}), because ectopic expression of a dominant-negative form of Cdc42 or distinct pharmacological PI3K inhibitors abrogated these responses. Furthermore, we demonstrate that BMP2 activates different group I and group II PAK isoforms as well as LIMK1 with similar kinetics to Cdc42 or PI3K activation. BMP2 activation of PAK and LIMK1, measured by either kinase activity or with antibodies raised against phosphorylated residues at their activation loops, were abolished by blocking PI3K-signaling pathways. Together, these findings suggest that Cdc42 and PI3K signals emanating from BMP receptors are involved in specific regulation of actin assembly and cell migration.

Key words: BMP, Cell migration, Actin cytoskeleton, PI3K, Cdc42


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