Document Detail

Optical control of protein activity by fluorescent protein domains.
MedLine Citation:
PMID:  23139335     Owner:  NLM     Status:  MEDLINE    
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.
Xin X Zhou; Hokyung K Chung; Amy J Lam; Michael Z Lin
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Science (New York, N.Y.)     Volume:  338     ISSN:  1095-9203     ISO Abbreviation:  Science     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-09     Completed Date:  2012-12-03     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  United States    
Other Details:
Languages:  eng     Pagination:  810-4     Citation Subset:  IM    
Department of Bioengineering, Stanford University, Stanford, CA 94305, USA.
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MeSH Terms
Adaptor Proteins, Vesicular Transport / chemistry,  genetics,  metabolism
Cell Membrane / metabolism
HeLa Cells
Luminescent Proteins / chemistry*,  genetics,  metabolism
Models, Molecular
NIH 3T3 Cells
Native Polyacrylamide Gel Electrophoresis
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
Reg. No./Substance:
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
Comment In:
Nat Methods. 2013 Jan;10(1):16   [PMID:  23547292 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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