| Optical control of protein activity by fluorescent protein domains. | |
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MedLine Citation:
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PMID: 23139335 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Xin X Zhou; Hokyung K Chung; Amy J Lam; Michael Z Lin |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Science (New York, N.Y.) Volume: 338 ISSN: 1095-9203 ISO Abbreviation: Science Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-11-09 Completed Date: 2012-12-03 Revised Date: 2013-04-01 |
Medline Journal Info:
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Nlm Unique ID: 0404511 Medline TA: Science Country: United States |
Other Details:
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Languages: eng Pagination: 810-4 Citation Subset: IM |
Affiliation:
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Department of Bioengineering, Stanford University, Stanford, CA 94305, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Vesicular Transport
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chemistry,
genetics,
metabolism Animals Cell Membrane / metabolism Darkness Fluorescence HeLa Cells Humans Light* Luminescent Proteins / chemistry*, genetics, metabolism Mice Models, Molecular NIH 3T3 Cells Native Polyacrylamide Gel Electrophoresis Optogenetics Protein Conformation Protein Engineering Protein Multimerization Protein Structure, Tertiary* Pseudopodia / metabolism, ultrastructure Recombinant Fusion Proteins / chemistry*, genetics, metabolism Serine Endopeptidases / chemistry, genetics, metabolism Viral Nonstructural Proteins / chemistry, genetics, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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R01NS076860/NS/NINDS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Vesicular Transport; 0/Luminescent Proteins; 0/NS3 protein, hepatitis C virus; 0/NS4 protein, hepatitis C virus; 0/Recombinant Fusion Proteins; 0/Viral Nonstructural Proteins; 0/intersectin 1; 0/neptune protein; EC 3.4.21.-/Serine Endopeptidases |
| Comments/Corrections | |
Comment In:
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Nat Methods. 2013 Jan;10(1):16 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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