Coordination of Rho GTPase activities during cell protrusion

Matthias Machacek, Louis Hodgson, Christopher Welch, Hunter Elliott, Olivier Pertz, Perihan Nalbant, Amy Abell, Gary L. Johnson, Klaus M. Hahn () and Gaudenz Danuser ()
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Matthias Machacek: The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA
Louis Hodgson: Medicinal Chemistry and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Christopher Welch: Medicinal Chemistry and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Hunter Elliott: The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA
Olivier Pertz: The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA
Perihan Nalbant: Center for Medical Biotechnology, University of Duisburg-Essen
Amy Abell: Medicinal Chemistry and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Gary L. Johnson: Medicinal Chemistry and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Klaus M. Hahn: Medicinal Chemistry and Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA
Gaudenz Danuser: The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA

Nature, 2009, vol. 461, issue 7260, 99-103

Abstract: Rho GTPases during cell protrusion The Rho GTPase family acts in concert to regulate cyoskeletal dynamics during processes such as cell motility. In this study, Danuser and colleagues study the coordination of RhoA, Rac1 and Cdc42 during cell migration by simultaneously visualizing two molecules using complementary biosensor designs, and by computationally defining the relationships between individual molecules visualized in separate cells. The latter approach demonstrates that different biosensors, imaged separately, can be freely combined to produce maps of relative signalling activities with seconds and single-micron resolution. These technologies pave the way to defining the dynamics of many proteins in large signal transduction networks.

Date: 2009
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DOI: 10.1038/nature08242

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