Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism
AMP-activated protein kinase AMPK senses and regulates cellular energy state. Here the authors engineer a synthetic sensor, AMPfret, that allows direct, real-time readout of the AMPK conformational state by fluorescence resonance energy transfer (FRET).
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2019-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-019-08938-z |
| _version_ | 1818419854988804096 |
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| author | Martin Pelosse Cécile Cottet-Rousselle Cécile M. Bidan Aurélie Dupont Kapil Gupta Imre Berger Uwe Schlattner |
| author_facet | Martin Pelosse Cécile Cottet-Rousselle Cécile M. Bidan Aurélie Dupont Kapil Gupta Imre Berger Uwe Schlattner |
| author_sort | Martin Pelosse |
| collection | DOAJ |
| description | AMP-activated protein kinase AMPK senses and regulates cellular energy state. Here the authors engineer a synthetic sensor, AMPfret, that allows direct, real-time readout of the AMPK conformational state by fluorescence resonance energy transfer (FRET). |
| first_indexed | 2024-12-14T12:45:12Z |
| format | Article |
| id | doaj.art-8d15448cd9064472a9bb9937a9aad01a |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T12:45:12Z |
| publishDate | 2019-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-8d15448cd9064472a9bb9937a9aad01a2022-12-21T23:00:48ZengNature PortfolioNature Communications2041-17232019-03-0110111310.1038/s41467-019-08938-zSynthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanismMartin Pelosse0Cécile Cottet-Rousselle1Cécile M. Bidan2Aurélie Dupont3Kapil Gupta4Imre Berger5Uwe Schlattner6University of Grenoble Alpes and INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), Rue de la Piscine, Domaine UniversitaireUniversity of Grenoble Alpes and INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), Rue de la Piscine, Domaine UniversitaireUniversity of Grenoble Alpes, CNRS, Laboratoire Interdisciplinaire de Physique (LIPhy)University of Grenoble Alpes, CNRS, Laboratoire Interdisciplinaire de Physique (LIPhy)Bristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, University of BristolBristol Synthetic Biology Centre BrisSynBio, Biomedical Sciences, University of BristolUniversity of Grenoble Alpes and INSERM U1055, Laboratory of Fundamental and Applied Bioenergetics (LBFA) and SFR Environmental and Systems Biology (BEeSy), Rue de la Piscine, Domaine UniversitaireAMP-activated protein kinase AMPK senses and regulates cellular energy state. Here the authors engineer a synthetic sensor, AMPfret, that allows direct, real-time readout of the AMPK conformational state by fluorescence resonance energy transfer (FRET).https://doi.org/10.1038/s41467-019-08938-z |
| spellingShingle | Martin Pelosse Cécile Cottet-Rousselle Cécile M. Bidan Aurélie Dupont Kapil Gupta Imre Berger Uwe Schlattner Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism Nature Communications |
| title | Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism |
| title_full | Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism |
| title_fullStr | Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism |
| title_full_unstemmed | Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism |
| title_short | Synthetic energy sensor AMPfret deciphers adenylate-dependent AMPK activation mechanism |
| title_sort | synthetic energy sensor ampfret deciphers adenylate dependent ampk activation mechanism |
| url | https://doi.org/10.1038/s41467-019-08938-z |
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