Abstract
More than a dozen years ago, Dr. Patrick Casey wrote a review for the Journal of Lipid Research (JLR) on a fledgling area of lipid biology: the biochemistry and enzymology of protein prenylation (1). His article and others on the same topic (2) stimulated interest in the posttranslational modification of proteins with lipids. During the past decade, there have been many advances in understanding lipid modifications of proteins, spanning not only enzymology and biochemistry, but also genetic and pharmacologic studies linking lipid modifications to the pathogenesis and treatment of human disease.
Highlights
More than a dozen years ago, Dr Patrick Casey wrote a review for the Journal of Lipid Research (JLR) on a fledgling area of lipid biology: the biochemistry and enzymology of protein prenylation (1)
The focus of our review will be the posttranslational processing of farnesylated protein in mammalian cells, prelamin A
Prelamin A terminates with a CAAX motif, which triggers farnesylation of a C-terminal cysteine, endoproteolytic release of the last three amino acids (AAX), and methylation of the newly exposed farnesylcysteine
Summary
More than a dozen years ago, Dr Patrick Casey wrote a review for the Journal of Lipid Research (JLR) on a fledgling area of lipid biology: the biochemistry and enzymology of protein prenylation (1). The focus of our review will be the posttranslational processing of farnesylated protein in mammalian cells, prelamin A. In the absence of ZMPSTE24, farnesyl-prelamin A accumulates in cells, causing misshapen cell nuclei and disease phenotypes resembling those in progeroid syndromes.
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