論文 - 詳細
| RRC ID | 77881 |
|---|---|
| 著者 | Suzuki S, Nakamura A, Hatano Y, Yoshikawa M, Yoshii T, Sawada S, Atsuta-Tsunoda K, Aoki K, Tsukiji S. |
| タイトル | A chemogenetic platform for controlling plasma membrane signaling and synthetic signal oscillation. |
| ジャーナル | Cell Chem Biol |
| Abstract |
Chemogenetic methods enabling the rapid translocation of specific proteins to the plasma membrane (PM) in a single protein-single ligand manner are useful tools in cell biology. We recently developed a technique, in which proteins fused to an Escherichia coli dihydrofolate reductase (eDHFR) variant carrying N-terminal hexalysine residues are recruited from the cytoplasm to the PM using the synthetic myristoyl-d-Cys-tethered trimethoprim (mDcTMP) ligand. However, this system achieved PM-specific translocation only when the eDHFR tag was fused to the N terminus of proteins, thereby limiting its application. In this report, we engineered a universal PM-targeting tag for mDcTMP-induced protein translocation by grafting the hexalysine motif into an intra-loop region of eDHFR. We demonstrate the broad applicability of the new loop-engineered eDHFR tag and mDcTMP pair for conditional PM recruitment and activation of various tag-fused signaling proteins with different fusion configurations and for reversibly and repeatedly controlling protein localization to generate synthetic signal oscillations. |
| 巻・号 | 29(9) |
| ページ | 1446-1464.e10 |
| 公開日 | 2022-9-15 |
| DOI | 10.1016/j.chembiol.2022.06.005 |
| PII | S2451-9456(22)00237-9 |
| PMID | 35835118 |
| MeSH | Cell Membrane / metabolism Escherichia coli / metabolism Ligands Proteins Signal Transduction Tetrahydrofolate Dehydrogenase* / metabolism Trimethoprim* / pharmacology |
| IF | 6.762 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 24 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 酵母 | FYP4993 |