<p>Chapter 1: Protein prenylation: A perspective on initial discoveries</p> <p>John Glomset</p> <p>Chapter 2: Insights into the function of prenylation from nuclear lamin farnesylation</p> <p>Michael Sinensky</p> <p>Chapter 3: Posttranslational Processing of Nuclear Lamins </p> <p>Brandon S. J. Davies, Catherine Coffinier, Shao H. Yang, Hea-Jin Jung, Loren G. Fong, and Stephen G. Young</p> <p>Chapter 4: Prenylated Proteins in Peroxisome Biogenesis</p> <p>Robert Rucktäschel, Rezeda Mirgalieva, Ralf Erdmann</p> <p>Chapter 5: Lipid Modification of Ras Superfamily GTPases: Not Just Membrane Glue</p> <p>Emily J. Chenette,<sup>, </sup>Channing J. Der</p> <p>Chapter 6: Heterogeneous Prenyl Processing of the Heterotrimeric G protein Gamma Subunits</p> <p>John Hildebrandt</p> <p>Chapter 7: Farnesylation versus geranylgeranylation in G-protein-mediated light signaling </p> <p>Masahiro Okada , Hidetoshi Kassai, Yoshitaka Fukada</p> <p>Chapter 8: Organization and function of the Rab prenylation and recycling machinery</p> <p>Kirill Alexandrov, Yaowen Wu, Wulf Blankenfeldt, Herbert Waldmann, Roger S. Goody<sup> </p></sup> <p>Chapter 9: Protein prenylation and CaaX processing in plants</p> <p>Shaul Yalovsky</p> <p>Chapter 10: Posttranslational isoprenylation on tryptophan residue in Bacillus subtilis</p> <p>Masahiro Okada, Fumitada Tsuji, Youji Sakagami</p> <p>Chapter 11: Global analysis of prenylated proteins by the use of a tagging via substrate approach</p> <p>Lai N. Chan, Fuyuhiko Tamanoi</p> <p>Chapter 12: Global Identification of Protein Prenyltransferase Substrates: Defining the Prenylated Proteome</p> <p>Corissa L. Lamphear, Elaina A. Zverina, James L. Hougland, Carol A. Fierke</p> <p>Chapter 13: Structural biochemistry of CaaX protein prenyltransferases</p> <p>Michael A. Hast , Lorena S. Beese</p> <p>Chapter 14: Genetic Analyses of the CAAX Protein Prenyltransferases in Mice</p> <p>MOHAMED X. IBRAHIM, OMAR M. KHAN, MARTIN O. BERGO</p> <p>Chapter 15: Farnesyl Transferase Inhibitors: From Targeted Cancer Therapeutic to a Potential Treatment for Progeria</p> <p>W. Robert Bishop, Ronald Doll, Paul Kirschmeier </p>