Summary of ssbd-repos-000177

SSBD:database
URL

Name
ssbd-repos-000177 (177-Kinjo-cAMPsignalingDyn)
URL
DOI
-

Title
Fluorescence images of the cAMP-Signaling Pathway in 3D Tissues with FRET-Assisted Two-Photon Activation of bPAC.
Description
-
Submited Date
-
Release Date
2022-03-31
Updated Date
-
License
Funding information
-
File formats
Data size
4.3 GB

Organism
Mus musculus, Homo sapiens, Canis lupus familiaris
Strain
-
Cell Line
MDCK cell, HeLa cell
Genes
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Proteins
TFP1

GO Molecular Function (MF)
NA
GO Biological Process (BP)
cAMP-mediated signaling
GO Cellular Component (CC)
cAMP-dependent protein kinase complex
Study Type
Biosensing Techniques/methods, Enzyme Activation, Adenylyl Cyclases, Biosensing Techniques, Signal Transduction, Cell Communication, Liver/metabolism, Green Fluorescent Proteins/metabolism, Humans, Fluorescent Dyes/metabolism, Bacteria, HeLa Cells, Dogs, Mice, Fluorescence Resonance Energy Transfer, Cyclic AMP, Fluorescent Dyes, Single-Cell Analysis/methods, Liver, Fluorescence Resonance Energy Transfer/methods, Single-Cell Analysis, Cyclic AMP-Dependent Protein Kinases, Animals, Madin Darby Canine Kidney Cells, Cyclic AMP-Dependent Protein Kinases/metabolism, Bacteria/enzymology, Cyclic AMP/metabolism, Adenylyl Cyclases/metabolism, Green Fluorescent Proteins
Imaging Methods
time lapse microscopy, FRET, differences in fluorescence lifetime

Method Summary
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Related paper(s)

Tomoaki Kinjo, Tetsuya Watabe, Kenju Kobachi, Kenta Terai, Michiyuki Matsuda (2020) Single-Cell Activation of the cAMP-Signaling Pathway in 3D Tissues with FRET-Assisted Two-Photon Activation of bPAC., ACS chemical biology, Volume 15, Number 11, pp. 2848-2853

Published in 2020 Nov 20 (Electronic publication in Oct. 19, 2020, midnight )

(Abstract) Bacterial photoactivated adenylyl cyclase (bPAC) has been widely used in signal transduction research. However, due to its low two-photon absorption, bPAC cannot be efficiently activated by two-photon (2P) excitation. Taking advantage of the high two-photon absorption of monomeric teal fluorescent protein 1 (mTFP1), we herein developed 2P-activatable bPAC (2pabPAC), a fusion protein consisting of bPAC and mTFP1. In 2pabPAC, the energy absorbed by mTFP1 excites bPAC by Furster resonance energy transfer (FRET) at ca. 43% efficiency. The light-induced increase in cAMP was monitored by a red-shifted FRET biosensor for PKA. In 3D MDCK cells and mouse liver, PKA was activated at single-cell resolution under a 2P microscope. We found that PKA activation in a single hepatocyte caused PKA activation in neighboring cells, indicating the propagation of PKA activation. Thus, 2pabPAC will provide a versatile platform for controlling the cAMP signaling pathway and investigating cell-to-cell communication in vivo.
(MeSH Terms)

Contact(s)
Kenta Terai
Organization(s)
Graduate School of Medicine, Kyoto University , Department of Pathology and Biology of Diseases
Image Data Contributors
Quantitative Data Contributors

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