Journal
SCIENCE
Volume 305, Issue 5690, Pages 1615-1619Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1100367
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Funding
- NIGMS NIH HHS [R01 GM057464, GM57464, GM64346] Funding Source: Medline
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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.
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