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Science 10 September 2004: Vol. 305. no. 5690, pp. 1615 - 1619 DOI: 10.1126/science.1100367
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Reports
Activation of Endogenous Cdc42 Visualized in Living Cells
Perihan Nalbant,*
Louis Hodgson,*
Vadim Kraynov,
Alexei Toutchkine,
Klaus M. Hahn
Signaling proteins are tightly regulated spatially and temporally to perform multiple functions. For Cdc42 and other guanosine triphosphatases, the subcellular location of activation is a critical determinant of cell behavior. However, current approaches are limited in their ability to examine the dynamics of Cdc42 activity in living cells. We report the development of a biosensor capable of visualizing the changing activation of endogenous, unlabeled Cdc42 in living cells. With the use of a dye that reports protein interactions, the biosensor revealed localized activation in the trans-Golgi apparatus, microtubule-dependent Cdc42 activation at the cell periphery, and activation kinetics precisely coordinated with cell extension and retraction.
Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill, NC 275997365, USA.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: khahn{at}med.unc.edu
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