Journal article
Temperature-responsive optogenetic probes of cell signaling
Nature chemical biology, v 18(2), pp 152-160
01 Feb 2022
PMID: 34937907
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
We describe single-component optogenetic probes whose activation dynamics depend on both light and temperature. We used the BcLOV4 photoreceptor to stimulate Ras and phosphatidyl inositol-3-kinase signaling in mammalian cells, allowing activation over a large dynamic range with low basal levels. Surprisingly, we found that BcLOV4 membrane translocation dynamics could be tuned by both light and temperature such that membrane localization spontaneously decayed at elevated temperatures despite constant illumination. Quantitative modeling predicted BcLOV4 activation dynamics across a range of light and temperature inputs and thus provides an experimental roadmap for BcLOV4-based probes. BcLOV4 drove strong and stable signal activation in both zebrafish and fly cells, and thermal inactivation provided a means to multiplex distinct blue-light sensitive tools in individual mammalian cells. BcLOV4 is thus a versatile photosensor with unique light and temperature sensitivity that enables straightforward generation of broadly applicable optogenetic tools.
The BcLOV4 photoreceptor was used to generate single-component optogenetic signaling probes whose activation dynamics are dependent on light and temperature, allowing multiplexing of blue-light-sensitive tools in mammalian cells
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Details
- Title
- Temperature-responsive optogenetic probes of cell signaling
- Creators
- William Benman - University of PennsylvaniaErin E. Berlew - University of PennsylvaniaHao Deng - University of PennsylvaniaCaitlyn Parker - University of PennsylvaniaIvan A. Kuznetsov - University of PennsylvaniaBomyi Lim - University of PennsylvaniaArndt F. Siekmann - University of PennsylvaniaBrian Y. Chow - University of PennsylvaniaLukasz J. Bugaj - California Institute for Regenerative Medicine
- Publication Details
- Nature chemical biology, v 18(2), pp 152-160
- Publisher
- Nature Publishing Group US
- Number of pages
- 9
- Grant note
- 2020268469; CAREER MCB1652003; CAREER MCB1652003 / National Science Foundation (NSF) (https://doi.org/10.13039/100000001) R01NS101106; R35GM133425; R35GM133425; R01HL152086; R35GM138211; R21GM132831 / Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) (https://doi.org/10.13039/100000009)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems
- Web of Science ID
- WOS:000733335800001
- Scopus ID
- 2-s2.0-85121594894
- Other Identifier
- 991022138678704721
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- Web of Science research areas
- Biochemistry & Molecular Biology