Abstract
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.
Original language | English (US) |
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Pages (from-to) | 1615-1619 |
Number of pages | 5 |
Journal | Science |
Volume | 305 |
Issue number | 5690 |
DOIs | |
State | Published - Sep 10 2004 |
Externally published | Yes |
ASJC Scopus subject areas
- General