ArticleACS synthetic biology2014
Control of protein function through optochemical translocation.
Article in ACS synthetic biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- Design principles for optogenetic-based targeted protein degradation.Synthetic and systems biotechnology · 2026Review
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic Biology.Chemical reviews · 2024Review
- Genetically Encoded Lysine Analogues with Differential Light Sensitivity for Activation of Protein Function.ChemPhotoChem · 2024Article
- Applications of genetic code expansion technology in eukaryotes.Protein & cell · 2024Review
- Genetically encoded lysine photocage for spatiotemporal control of TDP-43 nuclear import.Biophysical chemistry · 2024Article
- A chemical magnet: Approaches to guide precise protein localization.Bioorganic & medicinal chemistry · 2024Article
- Synthetic peptides for the precise transportation of proteins of interests to selectable subcellular areas.Frontiers in bioengineering and biotechnology · 2023Article
- Optogenetic control of YAP cellular localisation and function.EMBO reports · 2022Article
- Controlling Enzymatic Activity by Modulating the Oligomerization State via Chemical Rescue and Optical Control.Chembiochem : a European journal of chemical biology · 2022Article
- Optical Control of Phosphoinositide Binding: Rapid Activation of Subcellular Protein Translocation and Cell Signaling.ACS synthetic biology · 2021Article
- Protocol for photoactivation of YAP in cancer cell spheroids embedded in collagen gels.STAR protocols · 2021Article
- An optogenetic method for interrogating YAP1 and TAZ nuclear-cytoplasmic shuttling.Journal of cell science · 2021Article
- Spatio-selective activation of nuclear translocation of YAP with light directs invasion of cancer cell spheroids.iScience · 2021Article
- Optical control of MAP kinase kinase 6 (MKK6) reveals that it has divergent roles in pro-apoptotic and anti-proliferative signaling.The Journal of biological chemistry · 2020Article
- Phosphine-Activated Lysine Analogues for Fast Chemical Control of Protein Subcellular Localization and Protein SUMOylation.Chembiochem : a European journal of chemical biology · 2020Article
- Optical control of protein phosphatase function.Nature communications · 2019Article
- Using genetically incorporated unnatural amino acids to control protein functions in mammalian cells.Essays in biochemistry · 2019Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Controlled manipulation of proteins and their function is important in almost all biological disciplines. Here, we demonstrate control of protein activity with light. We present two different applications-light-triggered transcription and light-triggered protease cleavage-both based on the same concept of protein mislocation, followed by optochemically triggered translocation to an active cellular compartment. In our approach, we genetically encode a photocaged lysine into the nuclear localization signal (NLS) of the transcription factor SATB1. This blocks nuclear import of the protein until illumination induces caging group removal and release of the protein into the nucleus. In the first application, prepending this NLS to the transcription factor FOXO3 allows us to optochemically switch on its transcription activity. The second application uses the developed light-activated NLS to control nuclear import of TEV protease and subsequent cleavage of nuclear proteins containing TEV cleavage sites. The small size of the light-controlled NLS (only 20 amino acids) minimizes impact of its insertion on protein function and promises a general approach to a wide range of optochemical applications. Since the light-activated NLS is genetically encoded and optically triggered, it will prove useful to address a variety of problems requiring spatial and temporal control of protein function, for example, in stem-cell, developmental, and cancer biology.
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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.