Post-translational modification of proteins through the attachment of hydrophobic moieties has been shown to determine how proteins will be trafficked through the cell and where their final destination will be. Hydrophobic moieties including prenyl, myristate, palmitate and farnsyl groups signal translocation to the plasma membrane. The enzymatic addition of each group is controlled by a specific peptide sequence. We have mutated this sequence to incorporate a genetically engineered photocaged lysine amino acid. The caged lysine analog interferes with the post-translational modification and thus protein trafficking to the membrane, until it is activated through decaging with a brief UV irradiation. This precise temporal control allows for the calculation of the kinetics of the processing of post-translational modification and translocation of proteins in live cells.

Light-activation of protein membrane translocation in mammalian cells

243rd National Meeting (2012)

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