AI Article Synopsis
- Guanine-nucleotide dissociation inhibitors (GDIs) control Rho family GTPases by keeping them away from the cell membrane, which affects their activity in cell movement.
- The researchers developed a new biosensor called GDI.Cdc42 FLARE, using a technique that tracks Cdc42's activity by measuring fluorescence when it binds to GDIs.
- Their findings demonstrated a close coordination between the release and activation of Cdc42, indicating that GDI-Cdc42 interactions play a vital role in regulating Cdc42's activity and are important for the timing of cell movements.
Article Abstract
Guanine-nucleotide dissociation inhibitors (GDIs) are negative regulators of Rho family GTPases that sequester the GTPases away from the membrane. Here we ask how GDI-Cdc42 interaction regulates localized Cdc42 activation for cell motility. The sensitivity of cells to overexpression of Rho family pathway components led us to a new biosensor, GDI.Cdc42 FLARE, in which Cdc42 is modified with a fluorescence resonance energy transfer (FRET) 'binding antenna' that selectively reports Cdc42 binding to endogenous GDIs. Similar antennae could also report GDI-Rac1 and GDI-RhoA interaction. Through computational multiplexing and simultaneous imaging, we determined the spatiotemporal dynamics of GDI-Cdc42 interaction and Cdc42 activation during cell protrusion and retraction. This revealed remarkably tight coordination of GTPase release and activation on a time scale of 10 s, suggesting that GDI-Cdc42 interactions are a critical component of the spatiotemporal regulation of Cdc42 activity, and not merely a mechanism for global sequestration of an inactivated pool of signaling molecules.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5030135 | PMC |
| http://dx.doi.org/10.1038/nchembio.2145 | DOI Listing |
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