SIZ1-mediated SUMOylation during phosphate homeostasis in plants: Looking beyond the tip of the iceberg

Semin Cell Dev Biol. 2018 Feb:74:123-132. doi: 10.1016/j.semcdb.2017.09.016. Epub 2017 Sep 10.

Abstract

Availability of phosphate (Pi) is often limited in rhizospheres in different agroclimatic zones and adversely affects growth and development of plants. To circumvent this impasse, there is an urgent need and global consensus to develop Pi use efficient crops. To achieve this goal, it is essential to identify the molecular entities that exert regulatory influences on the sensing and signaling cascade governing Pi homeostasis. SIZ1 encodes a small ubiquitin-like modifier (SUMO E3) ligase, and plays a pivotal role in the post-translational SUMOylation of proteins. In this review, we discuss the reverse genetics approach conventionally used for providing circumstantial evidence towards the regulatory influences of SIZ1 on several morphophysiological and molecular traits that govern Pi homeostasis in taxonomically diverse Arabidopsis thaliana (Arabidopsis) and Oryza sativa (rice) model species. However, the efforts have been rather modest in identifying SUMO protein targets that play key roles in the maintenance of Pi homeostasis in these model plants contrary to the plethora of them now known in lower organisms and animals. Therefore, to predict the SIZ1-mediated SUMOylome involved in Pi homeostasis, the state-of-the-art high-throughput technologies often used for animals thus provide an attractive paradigm towards achieving the long-term goal of developing Pi use efficient crops.

Keywords: Arabidopsis thaliana (Arabidopsis); AtSIZ1 orthologs; Oryza sativa (rice); Phosphate (Pi) deficiency; Phylogenetic analysis; Post-translation modifications; SUMOylation; SUMOylation targets.

Publication types

  • Review

MeSH terms

  • Arabidopsis / chemistry
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / metabolism*
  • Homeostasis*
  • Ligases / metabolism*
  • Oryza / chemistry
  • Oryza / metabolism*
  • Phosphates / metabolism*
  • Sumoylation*

Substances

  • Arabidopsis Proteins
  • Phosphates
  • Ligases
  • SIZ1 protein, Arabidopsis