Plant protein kinase families and signal transduction

Julie M. Stone, John C. Walker

Research output: Contribution to journalReview articlepeer-review

352 Scopus citations

Abstract

Enzymes of the eukaryotic protein kinase superfamily catalyze the reversible transfer of the γ-phosphate from ATP to amino acid side chains of proteins. Protein kinase function can be counteracted by the action of phosphoprotein phosphatases. Phosphorylation status of a protein can have profound effects on its activity and interaction with other proteins. An estimated 1 to 3% of functional eukaryotic genes encode protein kinases, suggesting that they are involved in many aspects of cellular regulation and metabolism. In plants, protein phosphorylation has been implicated in responses to many signals, including light, pathogen invasion, hormones, temperature stress, and nutrient deprivation. Activities of several plant metabolic and regulatory enzymes are also controlled by reversible phosphorylation. As might be expected from this diversity of function, there is a large array of different protein kinases. Purification of protein kinases and their subsequent cloning, facilitated by the PCR and advances in homology-based cloning techniques, as well as functional analyses, including complementation of conditional yeast mutants and positional cloning of mutant plant genes, has already led to identification of more than 70 plant protein kinase genes. However, the precise functional roles of specific protein kinases and phosphatases during plant growth and development have been elucidated for only a few.

Original languageEnglish (US)
Pages (from-to)451-457
Number of pages7
JournalPlant physiology
Volume108
Issue number2
DOIs
StatePublished - Jun 1995

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science

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