Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 10 September 2004:
Vol. 305. no. 5690, pp. 1615 - 1619
DOI: 10.1126/science.1100367
Prev | Table of Contents | Next

Reports

Activation of Endogenous Cdc42 Visualized in Living Cells

Perihan Nalbant,* Louis Hodgson,* Vadim Kraynov, Alexei Toutchkine, Klaus M. Hahn{dagger}

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 27599–7365, USA.



* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: khahn{at}med.unc.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Endogenous Activation Patterns of Cdc42 GTPase Within Drosophila Embryos.
D. Kamiyama and A. Chiba (2009)
Science 324, 1338-1340
   Abstract »    Full Text »    PDF »
Live-cell microscopy - tips and tools.
M. M. Frigault, J. Lacoste, J. L. Swift, and C. M. Brown (2009)
J. Cell Sci. 122, 753-767
   Abstract »    Full Text »    PDF »
Models of Spatially Restricted Biochemical Reaction Systems.
S. R. Neves and R. Iyengar (2009)
J. Biol. Chem. 284, 5445-5449
   Abstract »    Full Text »    PDF »
Integrins in cell migration - the actin connection.
M. Vicente-Manzanares, C. K. Choi, and A. R. Horwitz (2009)
J. Cell Sci. 122, 199-206
   Abstract »    Full Text »    PDF »
Rapid Turnover Rate of Phosphoinositides at the Front of Migrating MDCK Cells.
T. Nishioka, K. Aoki, K. Hikake, H. Yoshizaki, E. Kiyokawa, and M. Matsuda (2008)
Mol. Biol. Cell 19, 4213-4223
   Abstract »    Full Text »    PDF »
Selective Labeling of Proteins with Chemical Probes in Living Cells.
M. Z. Lin and L. Wang (2008)
Physiology 23, 131-141
   Abstract »    Full Text »    PDF »
Controlling the rates of biochemical reactions and signaling networks by shape and volume changes.
L. Lizana, B. Bauer, and O. Orwar (2008)
PNAS 105, 4099-4104
   Abstract »    Full Text »    PDF »
The Tumor Suppressor LKB1 Regulates Lung Cancer Cell Polarity by Mediating cdc42 Recruitment and Activity.
S. Zhang, K. Schafer-Hales, F. R. Khuri, W. Zhou, P. M. Vertino, and A. I. Marcus (2008)
Cancer Res. 68, 740-748
   Abstract »    Full Text »    PDF »
Positive feedback between Cdc42 activity and H+ efflux by the Na-H exchanger NHE1 for polarity of migrating cells.
C. Frantz, A. Karydis, P. Nalbant, K. M. Hahn, and D. L. Barber (2007)
J. Cell Biol. 179, 403-410
   Abstract »    Full Text »    PDF »
Cdc42 is required for EGF-stimulated protrusion and motility in MTLn3 carcinoma cells.
M. El-Sibai, P. Nalbant, H. Pang, R. J. Flinn, C. Sarmiento, F. Macaluso, M. Cammer, J. S. Condeelis, K. M. Hahn, and J. M. Backer (2007)
J. Cell Sci. 120, 3465-3474
   Abstract »    Full Text »    PDF »
Filopodia formation via a specific Eph family member and PI3K in immortalized cholangiocytes.
K. Fukushima, Y. Ueno, J. Inoue, N. Kanno, and T. Shimosegawa (2006)
Am J Physiol Gastrointest Liver Physiol 291, G812-G819
   Abstract »    Full Text »    PDF »
The Rho-mDia1 Pathway Regulates Cell Polarity and Focal Adhesion Turnover in Migrating Cells through Mobilizing Apc and c-Src..
N. Yamana, Y. Arakawa, T. Nishino, K. Kurokawa, M. Tanji, R. E. Itoh, J. Monypenny, T. Ishizaki, H. Bito, K. Nozaki, et al. (2006)
Mol. Cell. Biol. 26, 6844-6858
   Abstract »    Full Text »    PDF »
From imaging to understanding: Frontiers in Live Cell Imaging, Bethesda, MD, April 19-21, 2006.
Y.-l. Wang, K. M. Hahn, R. F. Murphy, and A. F. Horwitz (2006)
J. Cell Biol. 174, 481-484
   Abstract »    Full Text »    PDF »
Targeting and activation of Rac1 are mediated by the exchange factor {beta}-Pix.
J. P. ten Klooster, Z. M. Jaffer, J. Chernoff, and P. L. Hordijk (2006)
J. Cell Biol. 172, 759-769
   Abstract »    Full Text »    PDF »
Cdc42 Induces Activation Loop Phosphorylation and Membrane Targeting of Mixed Lineage Kinase 3.
Y. Du, B. C. Bock, K. A. Schachter, M. Chao, and K. A. Gallo (2005)
J. Biol. Chem. 280, 42984-42993
   Abstract »    Full Text »    PDF »
Imaging Signal Transduction in Living Cells with Fluorescent Proteins.
M. R. Philips (2005)
Sci. STKE 2005, tr28
   Abstract »    Full Text »    PDF »
Polarized trafficking of E-cadherin is regulated by Rac1 and Cdc42 in Madin-Darby canine kidney cells.
B. Wang, F. G. Wylie, R. D. Teasdale, and J. L. Stow (2005)
Am J Physiol Cell Physiol 288, C1411-C1419
   Abstract »    Full Text »    PDF »
Concentric zones of active RhoA and Cdc42 around single cell wounds.
H. A. Benink and W. M. Bement (2005)
J. Cell Biol. 168, 429-439
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)