ArticleProceedings of the National Academy of Sciences of the United States of America2018
Light-activated protein interaction with high spatial subcellular confinement.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 105 citations in OpenAlex.
- An optogenetic toolkit for robust activation of FGF, BMP, & Nodal signaling in zebrafish.Developmental biology · 2026Article
- Technologies to measure and modulate protein subcellular localization.Nature reviews. Molecular cell biology · 2026Review
- Design principles for optogenetic-based targeted protein degradation.Synthetic and systems biotechnology · 2026Review
- Optogenetic Regulation of Localization and Function of Serotonin Transporter by Modulating Its Interaction with Soluble Guanylate Cyclase.International journal of molecular sciences · 2026Article
- A Single-Chain Light-Activatable Transcriptional Reporter for Fluorescently Tagging Mammalian Cells In Vitro.Chembiochem : a European journal of chemical biology · 2026Article
- Enhancing the performance of Magnets photosensors.Nature communications · 2026Article
- Traceless Regulation of Genetic Circuitry.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- How fungi see the world: fungal photoreceptors and their role in the regulation of fungal biology.Microbiology and molecular biology reviews : MMBR · 2025Review
- Two Decades of Optogenetic Tools: A Retrospective and a Look Ahead.Advanced genetics (Hoboken, N.J.) · 2025Review
- Chemogenetic and optogenetic strategies for spatiotemporal control of split-enzyme-based calcium recording.bioRxiv : the preprint server for biology · 2025Article
- Optogenetic control of receptor-mediated growth cone dynamics in neurons.Molecular biology of the cell · 2025Article
- Light-dependent modulation of protein localization and function in living bacteria cells.Nature communications · 2024Article
- Quantitative control of subcellular protein localization with a photochromic dimerizer.Nature chemical biology · 2024Article
- Endoplasmic reticulum exit sites are segregated for secretion based on cargo size.Developmental cell · 2024Article
- Optogenetics in Pancreatic Islets: Actuators and Effects.Diabetes · 2024Review
- Ultralow Background Membrane Editors for Spatiotemporal Control of Phosphatidic Acid Metabolism and Signaling.ACS central science · 2024Article
- Optogenetic Signaling Activation in Zebrafish Embryos.Journal of visualized experiments : JoVE · 2023Article
- Fluorogenic chemically induced dimerization.Nature methods · 2023Article
- Ultralow background membrane editors for spatiotemporal control of lipid metabolism and signaling.bioRxiv : the preprint server for biology · 2023Article
- Dimerization of iLID optogenetic proteins observed using 3D single-molecule tracking in live E. coli.Biophysical journal · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Methods to acutely manipulate protein interactions at the subcellular level are powerful tools in cell biology. Several blue-light-dependent optical dimerization tools have been developed. In these systems one protein component of the dimer (the bait) is directed to a specific subcellular location, while the other component (the prey) is fused to the protein of interest. Upon illumination, binding of the prey to the bait results in its subcellular redistribution. Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets. We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume. Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets. Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer. These findings highlight the distinct features of different optical dimerization systems and will be useful guides in the choice of tools for specific applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.