Caged Phosphopeptide-Based Approach for Photochemical Activation of Kinases in Living Cells

Kinase photoactivation: We have demonstrated that a caged analogue of SH2 domain‐binding phosphotyrosine peptide can be used as a tool for activating an intracellular phosphatidylinositol 3‐kinase (PI3K) by light. This approach should be generally applicable to other protein/lipid kinases of which t...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2008-07, Vol.9 (10), p.1583-1586
Main Authors: Kawakami, Takashi, Cheng, Huan, Hashiro, Shuhei, Nomura, Yasushi, Tsukiji, Shinya, Furuta, Toshiaki, Nagamune, Teruyuki
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
caged peptides
Enzyme Activation
Genes, Reporter
Green Fluorescent Proteins
kinases
Mice
Microinjections
Phosphatidylinositol 3-Kinases - metabolism
phospholipids
phosphopeptides
Phosphopeptides - chemistry
Phosphopeptides - metabolism
Phosphorylation
Photochemistry
Protein Kinases - metabolism
two-photon excitation
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Summary:Kinase photoactivation: We have demonstrated that a caged analogue of SH2 domain‐binding phosphotyrosine peptide can be used as a tool for activating an intracellular phosphatidylinositol 3‐kinase (PI3K) by light. This approach should be generally applicable to other protein/lipid kinases of which the catalytic activity is regulated by modular phosphopeptide‐binding domains.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200800116