Loading…
Phosphoproteome analyses pinpoint the F‐box protein SLOW MOTION as a regulator of warm temperature‐mediated hypocotyl growth in Arabidopsis
Summary Hypocotyl elongation is controlled by several signals and is a major characteristic of plants growing in darkness or under warm temperature. While already several molecular mechanisms associated with this process are known, protein degradation and associated E3 ligases have hardly been studi...
Saved in:
Published in: | The New phytologist 2024-01, Vol.241 (2), p.687-702 |
---|---|
Main Authors: | , , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Summary
Hypocotyl elongation is controlled by several signals and is a major characteristic of plants growing in darkness or under warm temperature. While already several molecular mechanisms associated with this process are known, protein degradation and associated E3 ligases have hardly been studied in the context of warm temperature.
In a time‐course phosphoproteome analysis on Arabidopsis seedlings exposed to control or warm ambient temperature, we observed reduced levels of diverse proteins over time, which could be due to transcription, translation, and/or degradation. In addition, we observed differential phosphorylation of the LRR F‐box protein SLOMO MOTION (SLOMO) at two serine residues.
We demonstrate that SLOMO is a negative regulator of hypocotyl growth, also under warm temperature conditions, and protein–protein interaction studies revealed possible interactors of SLOMO, such as MKK5, DWF1, and NCED4. We identified DWF1 as a likely SLOMO substrate and a regulator of warm temperature‐mediated hypocotyl growth.
We propose that warm temperature‐mediated regulation of SLOMO activity controls the abundance of hypocotyl growth regulators, such as DWF1, through ubiquitin‐mediated degradation. |
---|---|
ISSN: | 0028-646X 1469-8137 1469-8137 |
DOI: | 10.1111/nph.19383 |