Reversible Palmitoylierung von Proteinen

Biospektrum(2017)

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摘要
The covalent attachment of lipid moieties to proteins represents an important subclass of co- or post-translational modifications in the cell. The 16-carbon fully saturated lipid palmitate is preferentially conjugated to free cysteines of peripheral or integral membrane proteins. The thioester bond formed can be reversibly hydrolyzed and thereby modulates a proteins function with regard to trafficking, compartmentation within the membrane or lipid-induced conformational changes in a cyclic manner.
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