AI Article Synopsis
- Protein-protein interactions and localization are key for cellular signaling; controlling these interactions with chemical and optogenetic methods aids biological research and cell-based therapies.
- Current methods have limitations in precision, especially in light-scattering tissues, prompting the development of "thermomers"—temperature-controlled protein dimerization domains.
- Thermomers can reversibly manage protein association at specific temperatures (37-42 °C), allowing for precise control of protein interactions in various biological contexts.
Article Abstract
Protein-protein interactions and protein localization are essential mechanisms of cellular signal transduction. The ability to externally control such interactions using chemical and optogenetic methods has facilitated biological research and provided components for the engineering of cell-based therapies and materials. However, chemical and optical methods are limited in their ability to provide spatiotemporal specificity in light-scattering tissues. To overcome these limitations, we present "thermomers", modular protein dimerization domains controlled with temperature-a form of energy that can be delivered to cells both globally and locally in a wide variety of and contexts. Thermomers are based on a sharply thermolabile coiled-coil protein, which we engineered to heterodimerize at a tunable transition temperature within the biocompatible range of 37-42 °C. When fused to other proteins, thermomers can reversibly control their association, as demonstrated membrane localization in mammalian cells. This technology enables remote control of intracellular protein-protein interactions with a form of energy that can be delivered with spatiotemporal precision in a wide range of biological, therapeutic, and living material scenarios.
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| http://dx.doi.org/10.1021/acssynbio.9b00275 | DOI Listing |
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