The Metabolic Labeling and Analysis of Isoprenylated Proteins View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2002-02-19

AUTHORS

John M. Walker , 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 carboxyl-(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 has 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 that lack a transmembrane domain, and appear to be prerequisite for their in vivo activity (6,9,10). More... »

PAGES

657-672

Book

TITLE

Protein Protocols Handbook, The

ISBN

1-59259-169-8

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1385/1-59259-169-8:657

DOI

http://dx.doi.org/10.1385/1-59259-169-8:657

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007742111


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