AI Article Synopsis
- Researchers used optogenetics and chemogenetics to better understand protein signaling dynamics by creating allosteric switches that can be controlled with light or specific chemicals.* -
- They inserted sensory domains into specific, nonconserved areas of proteins, which allowed for precise control over the proteins' structural changes that dictate activity.* -
- This technique was successfully applied to motility signaling proteins, enabling the transformation between active and inactive states and influencing the behavior of living cells.*
Article Abstract
Optogenetic and chemogenetic control of proteins has revealed otherwise inaccessible facets of signaling dynamics. Here, we use light- or ligand-sensitive domains to modulate the structural disorder of diverse proteins, thereby generating robust allosteric switches. Sensory domains were inserted into nonconserved, surface-exposed loops that were tight and identified computationally as allosterically coupled to active sites. Allosteric switches introduced into motility signaling proteins (kinases, guanosine triphosphatases, and guanine exchange factors) controlled conversion between conformations closely resembling natural active and inactive states, as well as modulated the morphodynamics of living cells. Our results illustrate a broadly applicable approach to design physiological protein switches.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5362825 | PMC |
| http://dx.doi.org/10.1126/science.aah3404 | DOI Listing |
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