Journal
SCIENCE
Volume 344, Issue 6182, Pages 420-424Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1252367
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Funding
- National Institute of Mental Health
- Simons Foundation Autism Research Initiative
- National Institute on Drug Abuse
- Defense Advanced Research Projects Agency
- Gatsby Charitable Foundation
- Wiegers Family Fund
- German Academic Exchange Service (DAAD)
- Fidelity Foundation
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Using light to silence electrical activity in targeted cells is a major goal of optogenetics. Available optogenetic proteins that directly move ions to achieve silencing are inefficient, pumping only a single ion per photon across the cell membrane rather than allowing many ions per photon to flow through a channel pore. Building on high-resolution crystal-structure analysis, pore vestibule modeling, and structure-guided protein engineering, we designed and characterized a class of channelrhodopsins (originally cation-conducting) converted into chloride-conducting anion channels. These tools enable fast optical inhibition of action potentials and can be engineered to display step-function kinetics for stable inhibition, outlasting light pulses and for orders-of-magnitude-greater light sensitivity of inhibited cells. The resulting family of proteins defines an approach to more physiological, efficient, and sensitive optogenetic inhibition.
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