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Actin‐bundling protein fimbrin serves as a new auxin biosynthesis orchestrator in Arabidopsis root tips.

Authors :
Liu, Yan‐kun
Li, Jing‐jing
Xue, Qiao‐qiao
Zhang, Shu‐juan
Xie, Min
Cheng, Ting
Wang, Hong‐li
Liu, Cui‐mei
Chu, Jin‐fang
Pei, Yu‐sha
Jia, Bing‐qian
Li, Jia
Tian, Li‐jun
Fu, Ai‐gen
Hao, Ya‐qi
Su, Hui
Source :
New Phytologist; Oct2024, Vol. 244 Issue 2, p496-510, 15p
Publication Year :
2024

Abstract

Summary: Plants delicately regulate endogenous auxin levels through the coordination of transport, biosynthesis, and inactivation, which is crucial for growth and development. While it is well‐established that the actin cytoskeleton can regulate auxin levels by affecting polar transport, its potential role in auxin biosynthesis has remained largely unexplored.Using LC–MS/MS‐based methods combined with fluorescent auxin marker detection, we observed a significant increase in root auxin levels upon deletion of the actin bundling proteins AtFIM4 and AtFIM5. Fluorescent observation, immunoblotting analysis, and biochemical approaches revealed that AtFIM4 and AtFIM5 affect the protein abundance of the key auxin synthesis enzyme YUC8 in roots.AtFIM4 and AtFIM5 regulate the auxin synthesis enzyme YUC8 at the protein level, with its degradation mediated by the 26S proteasome. This regulation modulates auxin synthesis and endogenous auxin levels in roots, consequently impacting root development. Based on these findings, we propose a molecular pathway centered on the 'actin cytoskeleton‐26S proteasome‐YUC8‐auxin' axis that controls auxin levels.Our findings shed light on a new pathway through which plants regulate auxin synthesis. Moreover, this study illuminates a newfound role of the actin cytoskeleton in regulating plant growth and development, particularly through its involvement in maintaining protein homeostasis via the 26S proteasome. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0028646X
Volume :
244
Issue :
2
Database :
Complementary Index
Journal :
New Phytologist
Publication Type :
Academic Journal
Accession number :
180376195
Full Text :
https://doi.org/10.1111/nph.19959