Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications

Yen Chih Wang, Mark D. Distefano

Research output: Contribution to journalReview articlepeer-review

4 Scopus citations

Abstract

Protein prenylation is a posttranslational modification catalyzed by prenyltransferases involving the attachment of farnesyl or geranylgeranyl groups to residues near the C-termini of proteins. This irreversible covalent modification is important for membrane localization and proper signal transduction. Here, the use of isoprenoid analogues for studying prenylated proteins is reviewed. First, experiments with analogues containing small fluorophores that are alternative substrates for prenyltransferases are described. Those analogues have been useful for quantifying binding affinity and for the production of fluorescently labeled proteins. Next, the use of analogues that incorporate biotin, bioorthogonal groups or antigenic moieties is described. Such probes have been particularly useful for identifying proteins that are naturally prenylated within mammalian cells. Overall, the use of isoprenoid analogues has contributed significantly to the understanding of protein prenlation.

Original languageEnglish (US)
Pages (from-to)59-65
Number of pages7
JournalBioorganic Chemistry
Volume64
DOIs
StatePublished - Feb 1 2016

Bibliographical note

Funding Information:
This research was supported by the National Institutes of Health ( GM084152 and CA185783 ) and the National Science Foundation (CHE-1308655).

Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.

Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.

Keywords

  • Bioorthogonal labeling
  • Farnesylation
  • Fluorescent isoprenoids
  • Geranylgeranylation
  • Prenylomics
  • Protein prenylation
  • Proteomics

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