Membrane-localized ubiquitin ligase ATL15 functions in sugar-responsive growth regulation in Arabidopsis

Biochem Biophys Res Commun. 2017 Sep 9;491(1):33-39. doi: 10.1016/j.bbrc.2017.07.028. Epub 2017 Jul 6.

Abstract

Ubiquitin ligases play important roles in regulating various cellular processes by modulating the protein function of specific ubiquitination targets. The Arabidopsis Tóxicos en Levadura (ATL) family is a group of plant-specific RING-type ubiquitin ligases that localize to membranes via their N-terminal transmembrane-like domains. To date, 91 ATL isoforms have been identified in the Arabidopsis genome, with several ATLs reported to be involved in regulating plant responses to environmental stresses. However, the functions of most ATLs remain unknown. This study, involving transcriptome database analysis, identifies ATL15 as a sugar responsive ATL gene in Arabidopsis. ATL15 expression was rapidly down-regulated in the presence of sugar. The ATL15 protein showed ubiquitin ligase activity in vitro and localized to plasma membrane and endomembrane compartments. Further genetic analyses demonstrated that the atl15 knockout mutants are insensitive to high glucose concentrations, whereas ATL15 overexpression depresses plant growth. In addition, endogenous glucose and starch amounts were reciprocally affected in the atl15 knockout mutants and the ATL15 overexpressors. These results suggest that ATL15 protein plays a significant role as a membrane-localized ubiquitin ligase that regulates sugar-responsive plant growth in Arabidopsis.

Keywords: ATL family; Arabidopsis thaliana; Sugar; Ubiquitin ligase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / growth & development*
  • Arabidopsis Proteins / metabolism
  • Cell Membrane / enzymology*
  • Gene Expression Regulation, Plant / physiology
  • Glucose / metabolism*
  • Ubiquitin / metabolism*
  • Ubiquitin-Protein Ligases / metabolism*
  • Ubiquitination / physiology

Substances

  • Arabidopsis Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • Glucose