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The RING finger E3 ligase STRF1 is involved in membrane trafficking and modulates salt-stress response in Arabidopsis thaliana.
- Source :
- Plant Journal; Apr2015, Vol. 82 Issue 1, p81-92, 12p
- Publication Year :
- 2015
-
Abstract
- Salt stress is a detrimental factor for plant growth and development. The response to salt stress has been shown to involve components in the intracellular trafficking system, as well as components of the ubiquitin-proteasome system (UPS). In this article, we have identified in Arabidopsis thaliana a little reported ubiquitin ligase involved in salt-stress response, which we named STRF1 ( Salt Tolerance RING Finger 1). STRF1 is a member of RING-H2 finger proteins and we demonstrate that it has ubiquitin ligase activity in vitro. We also show that STRF1 localizes mainly at the plasma membrane and at the intracellular endosomes. strf1-1 loss-of-function mutant seedlings exhibit accelerated endocytosis in roots, and have altered expression of several genes involved in the membrane trafficking system. Moreover, protein trafficking inhibitor, brefeldin A (BFA), treatment has increased BFA bodies in strf1-1 mutant. This mutant also showed increased tolerance to salt, ionic and osmotic stresses, reduced accumulation of reactive oxygen species during salt stress, and increased expression of AtRbohD, which encodes a nicotinamide adenine dinucleotide phosphate (NADPH) oxidase involved in H<subscript>2</subscript>O<subscript>2</subscript> production. We conclude that STRF1 is a membrane trafficking-related ubiquitin ligase, which helps the plant to respond to salt stress by monitoring intracellular membrane trafficking and reactive oxygen species (ROS) production. [ABSTRACT FROM AUTHOR]
- Subjects :
- LIGASES
ARABIDOPSIS thaliana
UBIQUITIN
PROTEASOMES
ENDOSOMES
REACTIVE oxygen species
Subjects
Details
- Language :
- English
- ISSN :
- 09607412
- Volume :
- 82
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Plant Journal
- Publication Type :
- Academic Journal
- Accession number :
- 101713818
- Full Text :
- https://doi.org/10.1111/tpj.12797