4.7 Review

Jasmonate and auxin perception: how plants keep F-boxes in check

Journal

JOURNAL OF EXPERIMENTAL BOTANY
Volume 70, Issue 13, Pages 3401-3414

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/jxb/erz272

Keywords

Arabidopsis; coronatine; heat shock protein; JA-Ile; neddylation; polyubiquitination; post-translational modification; small molecule binding; ubiquitin-proteasome system; ubiquitination

Categories

Funding

  1. Research Foundation Flanders [G005915N]
  2. Swiss National Science Foundation [P300PA_177831]
  3. Swiss National Science Foundation (SNF) [P300PA_177831] Funding Source: Swiss National Science Foundation (SNF)

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Phytohormones regulate the plasticity of plant growth and development, and responses to biotic and abiotic stresses. Many hormone signal transduction cascades involve ubiquitination and subsequent degradation of proteins by the 26S proteasome. The conjugation of ubiquitin to a substrate is facilitated by the E1 activating, E2 conjugating, and the substrate-specifying E3 ligating enzymes. The most prevalent type of E3 ligase in plants is the Cullin-RING ligase (CRL)-type, with F-box proteins (FBPs) as the substrate recognition component. The activity of these SKP-Cullin-F-box (SCF) complexes needs to be tightly regulated in time and place. Here, we review the regulation of SCF function in plants on multiple levels, with a focus on the auxin and jasmonate SCF-type receptor complexes. We discuss in particular the relevance of protein-protein interactions and post-translational modifications as mechanisms to keep SCF functioning under control. Additionally, we highlight the unique property of SCFTIR1/AFB and SCFCOI1 to recognize substrates by forming co-receptor complexes. Finally, we explore how engineered selective agonists can be used to study and uncouple the outcomes of the complex auxin and jasmonate signaling networks that are governed by these FBPs.

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