ArticleNature chemical biology2024
Distinct phases of cellular signaling revealed by time-resolved protein synthesis.
Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A Protein Editing Method to Modify Proteins in Live Mammalian Cells.Current protocols · 2026Article
- Traceless protein semisynthesis in cells using the promiscuous ultra-fast split intein NrdJ-1.Chemical science · 2026Article
- Traceless protein semi-synthesis in cells using the promiscuous ultra-fast split intein NrdJ-1.bioRxiv : the preprint server for biology · 2026Article
- Alternative splicing in cancer drug resistance: Mechanisms and therapeutic prospects (Review).Oncology reports · 2026Review
- Programmable protein ligation on cell surfaces.Nature · 2025Article
- Int&in: A machine learning-based web server for active split site identification in inteins.Protein science : a publication of the Protein Society · 2024Article
- Cell surface sculpting using logic-gated protein actuators.bioRxiv : the preprint server for biology · 2023Article
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Abstract
The post-translational regulation of protein function is involved in most cellular processes. As such, synthetic biology tools that operate at this level provide opportunities for manipulating cellular states. Here we deploy proximity-triggered protein trans-splicing technology to enable the time-resolved synthesis of target proteins from premade parts. The modularity of the strategy allows for the addition or removal of various control elements as a function of the splicing reaction, in the process permitting the cellular location and/or activity state of starting materials and products to be differentiated. The approach is applied to a diverse set of proteins, including the kinase oncofusions breakpoint cluster region-Abelson (BCR-ABL) and DNAJ-PKAc where dynamic cellular phosphorylation events are dissected, revealing distinct phases of signaling and identifying molecular players connecting the oncofusion to cancer transformation as new therapeutic targets of cancer cells. We envision that the tools and control strategies developed herein will allow the activity of both naturally occurring and designer proteins to be harnessed for basic and applied research.
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