The tip of the iceberg: emerging roles of TORC1, and its regulatory functions in plant cells

J Exp Bot. 2021 May 18;72(11):4085-4101. doi: 10.1093/jxb/eraa603.

Abstract

Target of Rapamycin (TOR) is an evolutionarily conserved protein kinase that plays a central role in coordinating cell growth with light availability, the diurnal cycle, energy availability, and hormonal pathways. TOR Complex 1 (TORC1) controls cell proliferation, growth, metabolism, and defense in plants. Sugar availability is the main signal for activation of TOR in plants, as it also is in mammals and yeast. Specific regulators of the TOR kinase pathway in plants are inorganic compounds in the form of major nutrients in the soils, and light inputs via their impact on autotrophic metabolism. The lack of TOR is embryo-lethal in plants, whilst dysregulation of TOR signaling causes major alterations in growth and development. TOR exerts control as a regulator of protein translation via the action of proteins such as S6K, RPS6, and TAP46. Phytohormones are central players in the downstream systemic physiological TOR effects. TOR has recently been attributed to have roles in the control of DNA methylation, in the abundance of mRNA splicing variants, and in the variety of regulatory lncRNAs and miRNAs. In this review, we summarize recent discoveries in the plant TOR signaling pathway in the context of our current knowledge of mammalian and yeast cells, and highlight the most important gaps in our understanding of plants that need to be addressed in the future.

Keywords: Alternative splicing; DNA methylation; R2TPP complex; RNA regulation; TOR KINASE; TORC1 dimerization; Target of Rapamycin; hormonal regulation; plasmodesmata transport; protein translation; subcellular localization; sugar signaling.

Publication types

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

MeSH terms

  • Animals
  • Mechanistic Target of Rapamycin Complex 1
  • Plant Cells*
  • Plants / genetics
  • Protein Kinases
  • Signal Transduction*

Substances

  • Protein Kinases
  • Mechanistic Target of Rapamycin Complex 1