Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase.

@article{Inglese1992IsoprenylationOA,
  title={Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase.},
  author={James Inglese and J Fraser Glickman and W. Lorenz and Marc G. Caron and Robert J Lefkowitz},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 3},
  pages={1422-5}
}
The primary structure of bovine rhodopsin kinase (RK), which phosphorylates light-activated rhodopsin (Rho*), terminates with the amino acid sequence Cys558-Val-Leu-Ser561, a motif that has been shown to direct the isoprenylation and alpha-carboxyl methylation of many proteins (e.g. p21Ha-ras). Transient expression of RK in COS-7 cells revealed the presence of two immunoreactive protein species. Consistent with RK being modified by isoprenylation, interconversion of these two species was… CONTINUE READING

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