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The Biochemistry of Farnesyltransferase and Geranylgeranyltransferase I

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Farnesyltransferase Inhibitors in Cancer Therapy

Part of the book series: Cancer Drug Discovery and Development ((CDD&D))

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Abstract

Protein prenylation refers to a type of covalent posttranslational modification by lipids at cysteine residues near the C-terminus of a protein; either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid is attached to the protein via a thioether linkage (1–3) (Fig. 1). Protein prenylation is ubiquitous in the eukaryotic world, and most prenylated proteins are membrane-associated for at least part of their lifetime. The majority of prenylated proteins are involved in cellular signaling and/or regulatory events that occur at or near the cytoplasmic surfaces of cellular membranes (4,5).

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Authors
  1. Chih-Chin Huang PhD
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  2. Carol A. Fierke PhD
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  3. Patrick J. Casey PhD
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Editors and Affiliations

  1. H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, FL, USA

    Saïd M. Sebti PhD

  2. Department of Chemistry, Yale University, New Haven, CT, USA

    Andrew D. Hamilton PhD

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Huang, CC., Fierke, C.A., Casey, P.J. (2001). The Biochemistry of Farnesyltransferase and Geranylgeranyltransferase I. In: Sebti, S.M., Hamilton, A.D. (eds) Farnesyltransferase Inhibitors in Cancer Therapy. Cancer Drug Discovery and Development. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-013-1_2

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  • DOI: https://doi.org/10.1007/978-1-59259-013-1_2

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4684-9606-2

  • Online ISBN: 978-1-59259-013-1

  • eBook Packages: Springer Book Archive

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