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  AspSnFR: A genetically encoded biosensor for real-time monitoring of aspartate in live cells

Hellweg, L., Pfeifer, M., Tarnawski, M., Thing-Teoh, S., Chang, L., Bergner, A., et al. (2024). AspSnFR: A genetically encoded biosensor for real-time monitoring of aspartate in live cells. Cell Chemical Biology, 1-13. doi:10.1016/j.chembiol.2024.05.002.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000F-5DE0-C Version Permalink: https://hdl.handle.net/21.11116/0000-000F-5DE1-B
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Creators

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 Creators:
Hellweg, Lars1, Author           
Pfeifer, Martin, Author
Tarnawski, Miroslaw2, Author           
Thing-Teoh, Shao, Author
Chang, Lena, Author
Bergner, Andrea1, Author           
Kress, Jana1, Author           
Hiblot, Julien1, Author           
Wiedmer, Tabea, Author
Superti-Furga, Giulio, Author
Reinhardt, Jürgen, Author
Johnsson, Kai1, Author           
Leippe, Philipp1, Author           
Affiliations:
1Chemical Biology, Max Planck Institute for Medical Research, Max Planck Society, ou_2364732              
2Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: Aspartate is crucial for nucleotide synthesis, ammonia detoxification, and maintaining redox balance via the malate-aspartate-shuttle (MAS). To disentangle these multiple roles of aspartate metabolism, tools are required that measure aspartate concentrations in real time and in live cells. We introduce AspSnFR, a genetically encoded green fluorescent biosensor for intracellular aspartate, engineered through displaying and screening biosensor libraries on mammalian cells. In live cells, AspSnFR is able to precisely and quantitatively measure cytosolic aspartate concentrations and dissect its production from glutamine. Combining high-content imaging of AspSnFR with pharmacological perturbations exposes differences in metabolic vulnerabilities of aspartate levels based on nutrient availability. Further, AspSnFR facilitates tracking of aspartate export from mitochondria through SLC25A12, the MAS’ key transporter. We show that SLC25A12 is a rapidly responding and direct route to couple Ca2+ signaling with mitochondrial aspartate export. This establishes SLC25A12 as a crucial link between cellular signaling, mitochondrial respiration, and metabolism.

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Language(s): eng - English
 Dates: 2024-03-112024-01-182024-05-012024-05-27
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.chembiol.2024.05.002
 Degree: -

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Title: Cell Chemical Biology
Source Genre: Journal
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Publ. Info: Cell Press
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 1 - 13 Identifier: ISSN: 2451-9456
CoNE: https://pure.mpg.de/cone/journals/resource/2451-9456