title: LOVTRAP: an optogenetic system for photoinduced protein dissociation.
abstract: LOVTRAP is an optogenetic approach for reversible light-induced protein dissociation using protein A fragments that bind to the LOV domain only in the dark, with tunable kinetics and a >150-fold change in the dissociation constant (Kd). 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 proteins.
authors.affiliation: Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
authors.forename: Hui
authors.initials: H
authors.lastname: Wang
authors.affiliation: Lyda Hill Department of Bioinformatics, UT Southwestern Medical Center, Dallas, Texas, USA.
authors.forename: Marco
authors.initials: M
authors.lastname: Vilela
authors.affiliation: Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Winkler
authors.affiliation: Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
authors.forename: Miroslaw
authors.initials: M
authors.lastname: Tarnawski
authors.affiliation: Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
authors.forename: Ilme
authors.initials: I
authors.lastname: Schlichting
authors.affiliation: Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
authors.forename: Hayretin
authors.initials: H
authors.lastname: Yumerefendi
authors.affiliation: Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
authors.forename: Brian
authors.initials: B
authors.lastname: Kuhlman
authors.affiliation: Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.|Carolina Center for Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
authors.forename: Rihe
authors.initials: R
authors.lastname: Liu
authors.affiliation: Lyda Hill Department of Bioinformatics, UT Southwestern Medical Center, Dallas, Texas, USA.
authors.forename: Gaudenz
authors.initials: G
authors.lastname: Danuser
authors.affiliation: Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.|Lineberger Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
authors.forename: Klaus M
authors.initials: KM
authors.lastname: Hahn
mesh_terms: D018554:Avena / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D008027:Light; D062308:Optogenetics / Q000379:methods*; D058539:Phosphatidylinositol 3-Kinase / Q000737:chemistry* / Q000235:genetics / Q000528:radiation effects; D055519:Photoreceptors, Plant / Q000737:chemistry / Q000235:genetics / Q000528:radiation effects; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D051567:Proto-Oncogene Proteins c-vav / Q000737:chemistry* / Q000235:genetics / Q000528:radiation effects; D011993:Recombinant Fusion Proteins; D020830:rac1 GTP-Binding Protein / Q000737:chemistry* / Q000235:genetics / Q000528:radiation effects
chemical_list: D055519:Photoreceptors, Plant; D051567:Proto-Oncogene Proteins c-vav; C107953:RAC1 protein, human; D011993:Recombinant Fusion Proteins; C093651:VAV2 protein, human; D058539:Phosphatidylinositol 3-Kinase; D020830:rac1 GTP-Binding Protein