On the move: redox-dependent protein relocation in plants

Christine H. Foyer*, Alison Baker, Megan Wright, Imogen A. Sparkes, Amna Mhamdi, Jos H.M. Schippers, Frank Van Breusegem

*Corresponding author for this work

Research output: Contribution to journalReview article (Academic Journal)peer-review

39 Downloads (Pure)

Abstract

Compartmentation of proteins and processes is a defining feature of eukaryotic cells. The growth and development of organisms is critically dependent on the accurate sorting of proteins within cells. The mechanisms by which cytosol-synthesized proteins are delivered to the membranes and membrane compartments have been extensively characterized. However, the protein complement of any given compartment is not precisely fixed and some proteins can move between compartments in response to metabolic or environmental triggers. The mechanisms and processes that mediate such relocation events are largely uncharacterized. Many proteins can in addition perform multiple functions, catalysing alternative reactions or performing structural, non-enzymatic functions. These alternative functions can be equally important functions in each cellular compartment. Such proteins are generally not dual-targeted proteins in the classic sense of having targeting sequences that direct de novo synthesized proteins to specific cellular locations. We propose that redox post-translational modifications (PTMs) can control the compartmentation of many such proteins, including antioxidant and/or redox-associated enzymes.

Original languageEnglish
Article numbererz330
Pages (from-to)620-631
Number of pages12
JournalJournal of Experimental Botany
Volume71
Issue number2
Early online date17 Aug 2019
DOIs
Publication statusPublished - 7 Jan 2020

Keywords

  • Catalase
  • moonlighting proteins
  • nitric oxide
  • reactive oxygen species
  • redox signaling
  • stromules

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