Crosstalk between phosphorylation and O-GlcNAcylation: friend or foe

Research output: Contribution to journalReview article

Authors

Colleges, School and Institutes

External organisations

  • Bijvoet Center for Biomolecular Research
  • Netherlands Proteomics Centre

Abstract

A wide variety of protein post-translational modifications (PTMs) decorate cellular proteins, regulating their structure, interactions and ultimately their function. The density of co-occurring PTMs on proteins can be very high, where multiple PTMs can positively or negatively influence each other's actions, termed PTM crosstalk. In this review, we highlight recent progress in the area of PTM crosstalk, whereby we focus on crosstalk between protein phosphorylation and O-GlcNAcylation. These two PTMs largely target identical (i.e., Ser and Thr) amino acids in proteins. Phosphorylation/O-GlcNAcylation crosstalk comes in many flavors, for instance by competition for the same site/residue (reciprocal crosstalk), as well as by modifications influencing each other in proximity or even distal on the protein sequence. PTM crosstalk is observed on the writers of these modifications (i.e., kinases and O-GlcNAc transferase), on the erasers (i.e., phosphatases and O-GlcNAcase), and on the readers and the substrates. We describe examples of all these different flavors of crosstalk, and additionally the methods that are emerging to better investigate in particular phosphorylation/O-GlcNAcylation crosstalk.

Details

Original languageEnglish
Pages (from-to)3152-3167
Number of pages16
JournalFEBS Journal
Volume285
Issue number17
Early online date2 May 2018
Publication statusPublished - Sep 2018

Keywords

  • crosstalk, glycosylation, interplay, mass spectrometry, O-GlcNAcylation, phosphorylation, post-translational modifications, prediction, proteomics, signaling