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Science 13 October 2000:
Vol. 290. no. 5490, pp. 333 - 337
DOI: 10.1126/science.290.5490.333
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Reports

Localized Rac Activation Dynamics Visualized in Living Cells

Vadim S. Kraynov,1* Chester Chamberlain,1* Gary M. Bokoch,12 Martin A. Schwartz,3 Sarah Slabaugh,1 Klaus M. Hahn1dagger

Signaling proteins are thought to be tightly regulated spatially and temporally in order to generate specific and localized effects. For Rac and other small guanosine triphosphatases, binding to guanosine triphosphate leads to interaction with downstream targets and regulates subcellular localization. A method called FLAIR (fluorescence activation indicator for Rho proteins) was developed to quantify the spatio-temporal dynamics of the Rac1 nucleotide state in living cells. FLAIR revealed precise spatial control of growth factor-induced Rac activation, in membrane ruffles and in a gradient of activation at the leading edge of motile cells. FLAIR exemplifies a generally applicable approach for examining spatio-temporal control of protein activity.

Departments of
1 Cell Biology,
2 Immunology, and
3 Vascular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
*   These authors contributed equally to this work.

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

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   Abstract »    Full Text »    PDF »
Rac and Cdc42 play distinct roles in regulating PI(3,4,5)P3 and polarity during neutrophil chemotaxis.
S. Srinivasan, F. Wang, S. Glavas, A. Ott, F. Hofmann, K. Aktories, D. Kalman, and H. R. Bourne (2003)
J. Cell Biol. 160, 375-385
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Science. ISSN 0036-8075 (print), 1095-9203 (online)