Auxin-induced SCF TIR1 –Aux/IAA interaction involves stable modification of the SCF TIR1 complex
Open accessAbstract
The plant hormone auxin can regulate gene expression by destabilizing members of the Aux/IAA family of transcriptional repressors. Auxin-induced Aux/IAA degradation requires the protein-ubiquitin ligase SCF TIR1 , with auxin acting to enhance the interaction between the Aux/IAAs and SCF TIR1 . SKP1, Cullin, and an F-box-containing protein (SCF)-mediated degradation is an important component of many eukaryotic signaling pathways. In all known cases to date, the interaction between the targets and their cognate SCFs is regulated by signal-induced modification of the target. The mechanism by which auxin promotes the interaction between SCF TIR1 and Aux/IAAs is not understood, but current hypotheses propose auxin-induced phosphorylation, hydroxylation, or proline isomerization of the Aux/IAAs. We found no evidence to support these hypotheses or indeed that auxin induces any stable modification of Aux/IAAs to increase their affinity for SCF TIR1 . Instead, we present data suggesting that auxin promotes the SCF TIR1 –Aux/IAA interaction by affecting the SCF component, TIR1, or proteins tightly associated with it.
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Auxin acts by stabilizing the interaction between Aux/IAA proteins and the plant E3 ligase transport inhibitor response 1 (Tir1), promoting degradation of the Aux/IAA family of transcriptional repressors.
“Auxin acts by stabilizing the interaction between Aux/IAA proteins and the plant E3 ligase transport inhibitor response 1 (Tir1)239,240.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [240]
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- Authors
- Kepinski, S., & Leyser, O.
- Affiliations
- University of York (GB)
- Carnegie Institution for Science (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-08-04
- Volume
- 101
- Issue
- 33
- Pages
- 12381-12386
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC514484
- OpenAlex
- W2104585779
- Cited by
- 178
- References
- 20
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 5 · 2023: 5 · 2022: 14 · 2021: 3 · 2020: 6 · 2019: 11 · 2018: 2 · 2017: 5 · 2016: 3 · 2015: 5 · 2014: 5 · 2013: 7 · 2012: 5
- FWCI
- 20.01
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- auxin signaling, ubiquitination, protein degradation, TIR1, plant hormone signaling
- MeSH terms
- Amino Acid Sequence, Base Sequence, Benzamides, Indoleacetic Acids, Naphthols, Naphthoquinones, Recombinant Fusion Proteins, Arabidopsis, Protein Structure, Tertiary, DNA, Plant, Arabidopsis Proteins, Plants, Genetically Modified, SKP Cullin F-Box Protein Ligases, Macromolecular Substances
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