Improved synthetic lipidation-based protein translocation system for SNAP-tag fusion proteins

BioRxiv : the Preprint Server for Biology
T. YoshiiShinya Tsukiji


The ability to artificially attach lipids to specific intracellular protein targets would be a valuable approach for controlling protein localization and function in cells. We recently devised a chemogenetic method in which a SNAP-tag fusion protein can be translocated from the cytoplasm to the plasma membrane by post-translationally and covalently conjugating a synthetic lipopeptide in cells. However, the first-generation system lacked general applicability. Herein, we present an improved synthetic lipidation system that enables efficient plasma membrane translocation of SNAP-tag fusion proteins in cells. This second-generation system is now applicable to the control of various cell-signaling molecules, offering a new and useful research tool in chemical biology and synthetic biology.

Related Concepts

Untranslated Regions
Transcription, Genetic
Laboratory Round Trip
Nucleic Acid Sequencing
Protein Function
Protein Biosynthesis
Human Cell Line

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