AI Article Synopsis
- Many biological processes are influenced by how proteins interact and where they are located in the cell.
- The study introduces a new chemical inducer for protein dimerization that can be quickly activated or deactivated using specific light wavelengths.
- This new approach allows researchers to more precisely control cellular functions, like peroxisome transport and signaling during cell division, improving our understanding of protein interactions at the subcellular level.
Article Abstract
Many dynamic biological processes are regulated by protein-protein interactions and protein localization. Experimental techniques to probe such processes with temporal and spatial precision include photoactivatable proteins and chemically induced dimerization (CID) of proteins. CID has been used to study several cellular events, especially cell signaling networks, which are often reversible. However, chemical dimerizers that can be both rapidly activated and deactivated with high spatiotemporal resolution are currently limited. Herein, we present a novel chemical inducer of protein dimerization that can be rapidly turned on and off using single pulses of light at two orthogonal wavelengths. We demonstrate the utility of this molecule by controlling peroxisome transport and mitotic checkpoint signaling in living cells. Our system highlights and enhances the spatiotemporal control offered by CID. This tool addresses biological questions on subcellular levels by controlling protein-protein interactions.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6499933 | PMC |
| http://dx.doi.org/10.1021/jacs.8b07753 | DOI Listing |
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