@article {67178,
	title = {Optogenetic Tools for Manipulating Protein Subcellular Localization and Intracellular Signaling at Organelle Contact Sites},
	journal = {Current Protocols},
	volume = {1},
	year = {2021},
	month = {2021 Mar 03},
	abstract = {<p>Intracellular signaling processes are frequently based on direct interactions between proteins and organelles. A fundamental strategy to elucidate the physiological significance of such interactions is to utilize optical dimerization tools. These tools are based on the use of small proteins or domains that interact with each other upon light illumination. Optical dimerizers are particularly suitable for reproducing and interrogating a given protein-protein interaction and for investigating a protein{\textquoteright}s intracellular role in a spatially and temporally precise manner. Described in this article are genetic engineering strategies for the generation of modular light-activatable protein dimerization units and instructions for the preparation of optogenetic applications in mammalian cells. Detailed protocols are provided for the use of light-tunable switches to regulate protein recruitment to intracellular compartments, induce intracellular organellar membrane tethering, and reconstitute protein function using enhanced Magnets (eMags), a recently engineered optical dimerization system. {\textcopyright} 2021 Wiley Periodicals LLC.</p>
},
	issn = {2691-1299},
	doi = {https://doi.org/10.1002/cpz1.71},
	url = {https://doi.org/10.1002/cpz1.71},
	author = {Benedetti, Lorena}
}
@article {65827,
	title = {Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells.},
	journal = {Elife},
	volume = {9},
	year = {2020},
	month = {2020 Nov 11},
	abstract = {<p>Light-inducible dimerization protein modules enable precise temporal and spatial control of biological processes in non-invasive fashion. Among them, Magnets are small modules engineered from the photoreceptor Vivid by orthogonalizing the homodimerization interface into complementary heterodimers. Both Magnets components, which are well-tolerated as protein fusion partners, are photoreceptors requiring simultaneous photoactivation to interact, enabling high spatiotemporal confinement of dimerization with a single-excitation wavelength. However, Magnets require concatemerization for efficient responses and cell preincubation at 28C to be functional. Here we overcome these limitations by engineering an optimized Magnets pair requiring neither concatemerization nor low temperature preincubation. We validated these {\textquoteright}enhanced{\textquoteright} Magnets (eMags) by using them to rapidly and reversibly recruit proteins to subcellular organelles, to induce organelle contacts, and to reconstitute OSBP-VAP ER-Golgi tethering implicated in phosphatidylinositol-4-phosphate transport and metabolism. eMags represent a very effective tool to optogenetically manipulate physiological processes over whole cells or in small subcellular volumes.</p>
},
	issn = {2050-084X},
	doi = {10.7554/eLife.63230},
	author = {Benedetti, Lorena and Marvin, Jonathan S and Falahati, Hanieh and Guill{\'e}n-Samander, Andres and Looger, Loren L and De Camilli, Pietro}
}
