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 article

2 Citations (Scopus)

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

Fingerprint

Terpenes
Proteomics
Dimethylallyltranstransferase
Imaging techniques
Proteins
Protein Prenylation
Post Translational Protein Processing
Biotin
Protein C
Signal Transduction
Signal transduction
Fluorophores
Membranes
Cells
Substrates
Experiments

Keywords

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

Cite this

Synthetic isoprenoid analogues for the study of prenylated proteins : Fluorescent imaging and proteomic applications. / Wang, Yen Chih; Distefano, Mark D.

In: Bioorganic Chemistry, Vol. 64, 01.02.2016, p. 59-65.

Research output: Contribution to journalReview article

@article{7273b833fd634e509710bc08a24ad848,
title = "Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications",
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.",
keywords = "Bioorthogonal labeling, Farnesylation, Fluorescent isoprenoids, Geranylgeranylation, Prenylomics, Protein prenylation, Proteomics",
author = "Wang, {Yen Chih} and Distefano, {Mark D}",
year = "2016",
month = "2",
day = "1",
doi = "10.1016/j.bioorg.2015.12.003",
language = "English (US)",
volume = "64",
pages = "59--65",
journal = "Bioorganic Chemistry",
issn = "0045-2068",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Synthetic isoprenoid analogues for the study of prenylated proteins

T2 - Fluorescent imaging and proteomic applications

AU - Wang, Yen Chih

AU - Distefano, Mark D

PY - 2016/2/1

Y1 - 2016/2/1

N2 - 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.

AB - 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.

KW - Bioorthogonal labeling

KW - Farnesylation

KW - Fluorescent isoprenoids

KW - Geranylgeranylation

KW - Prenylomics

KW - Protein prenylation

KW - Proteomics

UR - http://www.scopus.com/inward/record.url?scp=84950267605&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84950267605&partnerID=8YFLogxK

U2 - 10.1016/j.bioorg.2015.12.003

DO - 10.1016/j.bioorg.2015.12.003

M3 - Review article

VL - 64

SP - 59

EP - 65

JO - Bioorganic Chemistry

JF - Bioorganic Chemistry

SN - 0045-2068

ER -