Regulation of plant peptide hormones and growth factors by post-translational modification

Publication Type

Journal contribution (peer reviewed)

Authors

Stührwohldt, N. and Schaller, A.

Year of publication

2018

Published in

Plant Biol.

Band/Volume

doi.org/10.1111/plb.12881/

DOI

10.1111/plb.12881

The number, the diversity and significance of peptides as regulators of cellular differentiation, growth, development, and defense of plants has long been underestimated. Peptides have now emerged as an important class of signaling molecules for cell-to-cell communication over short distances, and also for long-range signaling. We refer to them as peptide growth factors and peptide hormones, respectively. As compared to the remarkable progress with respect to the mechanisms of peptide perception and signal transduction, the biogenesis of signaling peptides is still in its infancy. This review focuses on the biogenesis and activity of small post-translationally modified peptides.  These peptides are derived from inactive pre-pro-peptides of approximately 70 to 120 amino acids. Multiple post-translational modifications (PTMs) may be required for peptide maturation and activation including proteolytic processing, tyrosine sulfation, proline hydroxylation and hydroxyproline glycosylation. While many of the enzymes responsible for these modifications have been identified, their impact on peptide activity and signaling is not fully understood. These PTMs may or may not be required for bioactivity, they may inactivate the peptide or modify its signaling specificity, they may affect peptide stability or targeting, or its binding affinity with the receptor. In the present review we will first introduce the peptides that undergo PTMs and for which these PTMs were shown to be functionally relevant. We will then discuss the different types of PTMs and the impact they have on peptide activity and plant growth and development. We conclude with an outlook on the open questions that need to be addressed in future research