Cutting in the middleman: hidden substrates at the interface between proteases and plant development

New Phytol. 2018 May;218(3):916-922. doi: 10.1111/nph.14501. Epub 2017 Mar 6.


Contents Summary 916 I. Introduction 916 II. DEK1: towards identification of protease substrates 917 III. Separases: when proteolytic modules attain nonproteolytic functions 918 IV. The peculiar case of a nonredundant subtilisin 919 V. Towards a solution to the protease redundancy problem 920 VI. Matters arising and closing remarks 921 Acknowledgements 921 References 921 SUMMARY: Proteases are integral components of proteome remodelling networks that regulate turnover of proteins and expand their functional diversity. Accumulating evidence highlights the importance of proteases as being central hubs of developmental programs. Yet the molecular pathways that many proteases act on, their natural substrates and their putative nonproteolytic functions remain largely elusive. Here, we discuss recent findings on proteases with functions that converge into plant development regulation, such as DEFECTIVE KERNEL 1 (DEK1), separase and subtilisins, to highlight conspicuous but unexplored aspects of protease biology. We also suggest an exploratory framework for addressing protease functions.

Keywords: asymmetric cell division; defective kernel; proteases; proteoforms; separase; serine proteases; subtilisin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Models, Biological
  • Peptide Hydrolases / metabolism*
  • Plant Development*
  • Proteolysis
  • Substrate Specificity


  • Peptide Hydrolases