caa a22 4500 467919909 CHVBK 20180406152914.0 cr unu---uuuuu 170328e20061001xx s 000 0 eng 10.1007/s00706-006-0534-9 doi (NATIONALLICENCE)springer-10.1007/s00706-006-0534-9 Protein Prenylation: An (Almost) Comprehensive Overview on Discovery History, Enzymology, and Significance in Physiology and Disease [Elektronische Daten] [Wolfgang Benetka, Manfred Koranda, Frank Eisenhaber] Summary.: Since 1979, when prenylation has been first discovered as chemical oddity of a yeast mating factor, the two forms of this posttranslational modification of proteins (farnesylation and geranylgeranylation) have been found as wide spread among proteins from Eukarya and their viruses. This review attempts to summarize as comprehensively as possible the enzymological processes of prenylation and the various aspects of their biological significance. The substrate proteins of prenyltransferases are known to carry a sequence signal composed of a cysteine-containing 4-5 residue stretch at the utmost C-terminal end that is N-terminally preceded by a flexible and polar linker region of ca. 10 residues. Postprenylation processing of substrate proteins can involve C-terminal proteolysis, C-terminal carboxyl methylation, and other steps of maturation. The prenyl anchor functions as module for membrane attachment or for protein-protein interaction. Prenyl anchor carrying proteins fulfill a large array of functions in signaling and regulation of cellular processes. Therefore, they are involved in the pathogenesis of a variety of human diseases, the most prominent one being cancer. Farnesyltransferase inhibitors show surprisingly high efficiency in controlling tumor growth in model systems but, so far, clinical trials with human patients have remained without the desired success. Interference into prenylation pathways appears also a promising treatment principle in a variety of parasitic diseases. Springer-Verlag, 2006 Keywords. Farnesyl nationallicence Geranylgeranyl nationallicence Prenyl nationallicence Farnesyltransferase inhibitor nationallicence Cancer nationallicence Parasitic disease nationallicence Benetka Wolfgang Research Institute of Molecular Pathology (IMP), Vienna, Austria aut Koranda Manfred Research Institute of Molecular Pathology (IMP), Vienna, Austria aut Eisenhaber Frank Research Institute of Molecular Pathology (IMP), Vienna, Austria aut Monatshefte für Chemie / Chemical Monthly Springer-Verlag 137/10(2006-10-01), 1241-1281 0026-9247 137:10<1241 2006 137 706 https://doi.org/10.1007/s00706-006-0534-9 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00706-006-0534-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Benetka Wolfgang Research Institute of Molecular Pathology (IMP), Vienna, Austria aut NATIONALLICENCE 700 1- Koranda Manfred Research Institute of Molecular Pathology (IMP), Vienna, Austria aut NATIONALLICENCE 700 1- Eisenhaber Frank Research Institute of Molecular Pathology (IMP), Vienna, Austria aut NATIONALLICENCE 773 0- Monatshefte für Chemie / Chemical Monthly Springer-Verlag 137/10(2006-10-01), 1241-1281 0026-9247 137:10<1241 2006 137 706 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer