LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation

Here we introduce LOVTRAP, an optogenetic approach for reversible, light-induced protein dissociation. LOVTRAP is based on protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in K(d). By reversibly sequestering proteins at mitochondria, w...

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Autores principales: Wang, Hui, Vilela, Marco, Winkler, Andreas, Tarnawski, Miroslaw, Schlichting, Ilme, Yumerefendi, Hayretin, Kuhlman, Brian, Liu, Rihe, Danuser, Gaudenz, Hahn, Klaus M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5137947/
https://www.ncbi.nlm.nih.gov/pubmed/27427858
http://dx.doi.org/10.1038/nmeth.3926
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author Wang, Hui
Vilela, Marco
Winkler, Andreas
Tarnawski, Miroslaw
Schlichting, Ilme
Yumerefendi, Hayretin
Kuhlman, Brian
Liu, Rihe
Danuser, Gaudenz
Hahn, Klaus M
author_facet Wang, Hui
Vilela, Marco
Winkler, Andreas
Tarnawski, Miroslaw
Schlichting, Ilme
Yumerefendi, Hayretin
Kuhlman, Brian
Liu, Rihe
Danuser, Gaudenz
Hahn, Klaus M
author_sort Wang, Hui
collection PubMed
description Here we introduce LOVTRAP, an optogenetic approach for reversible, light-induced protein dissociation. LOVTRAP is based on protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in K(d). By reversibly sequestering proteins at mitochondria, we precisely modulated the proteins’ access to the cell edge, demonstrating a naturally occurring 3 mHz cell edge oscillation driven by interactions of Vav2, Rac1 and PI3K.
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spelling pubmed-51379472017-01-18 LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation Wang, Hui Vilela, Marco Winkler, Andreas Tarnawski, Miroslaw Schlichting, Ilme Yumerefendi, Hayretin Kuhlman, Brian Liu, Rihe Danuser, Gaudenz Hahn, Klaus M Nat Methods Article Here we introduce LOVTRAP, an optogenetic approach for reversible, light-induced protein dissociation. LOVTRAP is based on protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in K(d). By reversibly sequestering proteins at mitochondria, we precisely modulated the proteins’ access to the cell edge, demonstrating a naturally occurring 3 mHz cell edge oscillation driven by interactions of Vav2, Rac1 and PI3K. 2016-07-18 2016-09 /pmc/articles/PMC5137947/ /pubmed/27427858 http://dx.doi.org/10.1038/nmeth.3926 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Wang, Hui
Vilela, Marco
Winkler, Andreas
Tarnawski, Miroslaw
Schlichting, Ilme
Yumerefendi, Hayretin
Kuhlman, Brian
Liu, Rihe
Danuser, Gaudenz
Hahn, Klaus M
LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation
title LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation
title_full LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation
title_fullStr LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation
title_full_unstemmed LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation
title_short LOVTRAP, An Optogenetic System for Photo-induced Protein Dissociation
title_sort lovtrap, an optogenetic system for photo-induced protein dissociation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5137947/
https://www.ncbi.nlm.nih.gov/pubmed/27427858
http://dx.doi.org/10.1038/nmeth.3926
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