Optical control of protein activity by fluorescent protein domains.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 23139335.
- Also identified by DOI 10.1126/science.1226854 and PMC identifier 3702057.
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Abstract
Fluorescent proteins (FPs) are widely used as optical sensors, whereas other light-absorbing domains have been used for optical control of protein localization or activity. Here, we describe light-dependent dissociation and association in a mutant of the photochromic FP Dronpa, and we used it to control protein activities with light. We created a fluorescent light-inducible protein design in which Dronpa domains are fused to both termini of an enzyme domain. In the dark, the Dronpa domains associate and cage the protein, but light induces Dronpa dissociation and activates the protein. This method enabled optical control over guanine nucleotide exchange factor and protease domains without extensive screening. Our findings extend the applications of FPs from exclusively sensing functions to also encompass optogenetic control.
Medical subject headings
- Adaptor Proteins, Vesicular Transport
- Adaptor Proteins, Vesicular Transport/chemistry
- Adaptor Proteins, Vesicular Transport/genetics
- Adaptor Proteins, Vesicular Transport/metabolism
- Animals
- Cell Membrane
- Cell Membrane/metabolism
- Darkness
- Fluorescence
- HeLa Cells
- Humans
- Light
- Luminescent Proteins
- Luminescent Proteins/chemistry
- Luminescent Proteins/genetics
- Luminescent Proteins/metabolism
- Mice
- Models, Molecular
- NIH 3T3 Cells
- Native Polyacrylamide Gel Electrophoresis
- Optogenetics
- Protein Conformation
- Protein Engineering
- Protein Multimerization
- Protein Structure, Tertiary
- Pseudopodia
- Pseudopodia/metabolism
- Pseudopodia/ultrastructure
- Recombinant Fusion Proteins
- Recombinant Fusion Proteins/chemistry
- Recombinant Fusion Proteins/genetics
- Recombinant Fusion Proteins/metabolism
- Serine Endopeptidases
- Serine Endopeptidases/chemistry
- Serine Endopeptidases/genetics
- Serine Endopeptidases/metabolism
- Viral Nonstructural Proteins
- Viral Nonstructural Proteins/chemistry
- Viral Nonstructural Proteins/genetics
- Viral Nonstructural Proteins/metabolism
- Nucleoside-Triphosphatase
- DEAD-box RNA Helicases
- Viral Proteases