z-logo
Premium
Protein farnesylation negatively regulates brassinosteroid signaling via reducing BES1 stability in Arabidopsis thaliana
Author(s) -
Feng Zengxiu,
Shi Hongyong,
Lv Minghui,
Ma Yuang,
Li Jia
Publication year - 2021
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.13093
Subject(s) - brassinosteroid , biology , arabidopsis , mutant , prenylation , endoplasmic reticulum , microbiology and biotechnology , transcription factor , signal transduction , arabidopsis thaliana , biochemistry , gene , enzyme
Brassinosteroids (BRs) are a group of steroidal phytohormones, playing critical roles in almost all physiological aspects during the life span of a plant. In Arabidopsis , BRs are perceived at the cell surface, triggering a reversible phosphorylation‐based signaling cascade that leads to the activation and nuclear accumulation of a family of transcription factors, represented by BES1 and BZR1. Protein farnesylation is a type of post‐translational modification, functioning in many important cellular processes. Previous studies demonstrated a role of farnesylation in BR biosynthesis via regulating the endoplasmic reticulum localization of a key bassinolide (BL) biosynthetic enzyme BR6ox2. Whether such a process is also involved in BR signaling is not understood. Here, we demonstrate that protein farnesylation is involved in mediating BR signaling in Arabidopsis . A loss‐of‐function mutant of ENHANCED RESPONSE TO ABA 1 ( ERA1 ), encoding a β subunit of the protein farnesyl transferase holoenzyme, can alter the BL sensitivity of bak1‐4 from a reduced to a hypersensitive level. era1 can partially rescue the BR defective phenotype of a heterozygous mutant of bin2‐1 , a gain‐of‐function mutant of BIN2 which encodes a negative regulator in the BR signaling. Our genetic and biochemical analyses revealed that ERA1 plays a significant role in regulating the protein stability of BES1.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here