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Background
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FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence.
FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.
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Background
References
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- Wang, T., et al., Science 271(5252):1120-1122 (1996).
- Zhang, F.L., et al., J. Biol. Chem. 269(5):3175-3180 (1994).
- Andres, D.A., et al., Genomics 18(1):105-112 (1993).
- Omer, C.A., et al., Biochemistry 32(19):5167-5176 (1993).
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