Rapid Identification of Cysteine-Linked Isoprenyl Groups by Metabolic Labeling with [<sup>3</sup>H]Farnesol and [<sup>3</sup>H]Geranylgeraniol View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999-05-20

AUTHORS

Michael H. Gelb , Douglas A. Andres , Dean C. Crick , Brian S. Finlin , Charles J. Waechter

ABSTRACT

The posttranslational modification of proteins by the covalent attachment of farnesyl and geranylgeranyl groups to cysteine residues at or near the C-terminus via a thioether bond is now well established in mammalian cells (1–6). Most isoprenylated proteins are thought to serve as regulators of cell signaling and membrane trafficking. Farnesylation and geranylgeranylation of the cysteinyl residues have been shown to promote both protein-protein and protein-membrane interactions (6–8). Isoprenylation, and, in some cases, the subsequent palmitoylation, provide a mechanism for the membrane association of polypeptides, which lack a transmembrane domain, and appear to be prerequisite for their in vivo activity (6,9,10). More... »

PAGES

107-124

Book

TITLE

Protein Lipidation Protocols

ISBN

1-59259-264-3

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1385/1-59259-264-3:107

DOI

http://dx.doi.org/10.1385/1-59259-264-3:107

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017121470


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