Phosphoproteomics as a tool to unravel plant regulatory mechanisms

Sergio De La Fuente Van Bentem, Elisabeth Roitinger, Dorothea Anrather, Edina Csaszar, Heribert Hirt*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

35 Scopus citations

Abstract

Reversible phosphorylation of proteins plays a key role in many regulatory processes that lie at the basis of life. With plants, much research has focused on protein kinases that are involved in the adaptation to different stress conditions, such as pathogen attack and cold. However, the substrates of these kinases are mostly unknown. With the recent advances in phosphoproteomic techniques, the large-scale identification of kinase substrates, including their phosphorylation sites, is finally possible. Studies in mainly non-plant systems have demonstrated the high potential of this method by uncovering numerous novel phosphorylation events. In this minireview, we focus on recent developments in the field of phosphoproteomics that are based on phosphopeptide isolation from complex mixtures by immobilized metal-affinity chromatography coupled to sequence identification by mass spectrometry. Combination of these methods with labelling techniques now allows quantitative analysis of phosphorylation between different samples. We discuss the potential of this technology to uncover entire phosphoproteomes and signalling pathways in plants in the future.

Original languageEnglish (US)
Pages (from-to)110-119
Number of pages10
JournalPhysiologia Plantarum
Volume126
Issue number1
DOIs
StatePublished - Jan 1 2006

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science
  • Cell Biology

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