Bioorthogonal metabolic labelling with acyl-CoA reporters: targeting protein acylation

Maria E. Ourailidou, Martijn R.H. Zwinderman, Frans Dekker

Research output: Contribution to journalReview articleAcademicpeer-review

3 Citations (Scopus)

Abstract

Protein acylation is an abundant post-translational modification with a pivotal role in a plethora of biological processes. To date, metabolic labelling with functionalized precursors of acyl-CoA and subsequent bio-orthogonal ligation to a complementary detection tag has offered an attractive approach for monitoring endogenous protein acylation with excellent selectivity. This review focuses on the applications of alkyne- and alkene-based bioorthogonal chemistries in the study of enzyme activity in vitro and summarizes the carboxylate-type chemical reporters that have enabled the visualization and identification of cellular acylated proteins. However, despite their importance, serious limitations question the use of this two-step labelling method in the quantification of the protein acylome.

Original languageEnglish
Pages (from-to)399-408
Number of pages10
JournalMedChemCommun
Volume7
Issue number3
DOIs
Publication statusPublished - 2016

Keywords

  • CYTOSOLIC ACETYL-COENZYME
  • OXIDATIVE HECK REACTION
  • 1,3-DIPOLAR CYCLOADDITION REACTION
  • ATP-CITRATE LYASE
  • CHEMICAL REPORTERS
  • CLICK CHEMISTRY
  • FATTY-ACIDS
  • POSTTRANSLATIONAL MODIFICATIONS
  • TERMINAL ALKYNES
  • HISTONE ACETYLTRANSFERASES

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