Posttranslational modification of proteins by isoprenoids in mammalian cells

@article{Maltese1990PosttranslationalMO,
  title={Posttranslational modification of proteins by isoprenoids in mammalian cells},
  author={William A Maltese},
  journal={The FASEB Journal},
  year={1990},
  volume={4},
  pages={3319 - 3328}
}
  • W. Maltese
  • Published 1 December 1990
  • Biology, Chemistry
  • The FASEB Journal
Isoprenylation is a posttranslational modification that involves the formation of thioether bonds between cysteine and isoprenyl groups derived from pyrophosphate intermediates of the cholesterol biosynthetic pathway. Numerous isoprenylated proteins have been detected in mammalian cells. Those identified include K‐, N‐, and H‐p21ras, ras‐related GTP‐binding proteins such as G25K (Gp), nuclear lamin B and prelamin A, and the γ subunits of heterotrimeric G proteins. The modified cysteine is… 
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Chemical biology of protein isoprenylation/methylation.
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Identification of an isoprenylated cysteine methyl ester hydrolase activity in bovine rod outer segment membranes.
TLDR
It is demonstrated here that simple isoprenylated cysteine derivatives, such as L-AFCM, L-AGGCM, and ebelactone B all inhibit the demethylation of the endogenous ROS substrates, showing that the same enzymatic activity is involved in the processing of the synthetic and physiological substrates.
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References

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G protein gamma subunits contain a 20-carbon isoprenoid.
TLDR
Isoprenylation of gamma subunits by the geranylgeranyl group is presumed to contribute to the association of G proteins with membranes.
p21ras is modified by a farnesyl isoprenoid.
TLDR
It is reported that the processing of ras proteins involves addition of a farnesyl moiety, apparently at the COOH-terminal Cysteine analogous to the cysteine modified in the yeast peptides, and that farNESylation may be important for membrane association and transforming activity of rAS proteins.
Characterization of isoprenoid involved in the post-translational modification of mammalian cell proteins.
TLDR
It is suggested that farnesylation of cysteine residues accounts for the well documented incorporation of mevalonic acid into mammalian cell proteins.
Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C‐terminal CXXM motif.
TLDR
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Isoprenylation is required for the processing of the lamin A precursor
TLDR
Analysis of the conversion of prelamin A to lamin A by two independent methods, immunoprecipitation and two-dimensional nonequilibrium pH gel electrophoresis, demonstrates that a precursor-product relationship exists between prelam in A and lamin B.
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