期刊
CHEMISTRY & BIOLOGY
卷 20, 期 4, 页码 549-557出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2013.03.010
关键词
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资金
- Swiss National Science Foundation [205320-138302, 31EM30-126143]
- ESF EuroMEMBRANE programme [FP-018]
- Novartis (Jubilee) Foundation
- Swiss National Science Foundation (SNF) [205320_138302, 31EM30-126143] Funding Source: Swiss National Science Foundation (SNF)
Cell activation initiated by receptor ligands or oncogenes triggers complex and convoluted intracellular signaling. Techniques initiating signals at defined starting points and cellular locations are attractive to elucidate the output of selected pathways. Here, we present the development and validation of a protein heterodimerization system based on small molecules cross-linking fusion proteins derived from Halo Tags and SNAP-tags. Chemical dimerizers of Halo Tag and SNAP-tag (HaXS) show excellent selectivity and have been optimized for intracellular reactivity. HaXS force protein-protein interactions and can translocate proteins to various cellular compartments. Due to the covalent nature of the HaloTag-HaXS-SNAP-tag complex, intracellular dimerization can be easily monitored. First applications include protein targeting to cytoskeleton, to the plasma membrane, to lysosomes, the initiation of the PI3K/mTOR pathway, and multiplexed protein complex formation in combination with the rapamycin dimerization system.
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