Auxin Perception--Structural Insights
Open accessAbstract
The identity of the auxin receptor(s) and the mechanism of auxin perception has been a subject of intense interest since the discovery of auxin almost a century ago. The development of genetic approaches to the study of plant hormone signaling led to the discovery that auxin acts by promoting degradation of transcriptional repressors called Aux/IAA proteins. This process requires a ubiquitin protein ligase (E3) called SCF(TIR1) and related SCF complexes. Surprisingly, auxin works by directly binding to TIR1, the F-box protein subunit of this SCF. Structural studies demonstrate that auxin acts like a "molecular glue," to stabilize the interaction between TIR1 and the Aux/IAA substrate. These exciting results solve an old problem in plant biology and reveal new mechanisms for E3 regulation and hormone perception.
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Auxin fills a gap between the E3 ligase and the degron motif of its substrate, complementing a suboptimal protein-protein interface, rather than allosterically inducing conformational changes in TIR1.
“Instead of allosterically inducing conformational changes in the F-box protein TIR1, auxin fills a gap between the E3 ligase and the degron motif of its substrate, complementing a suboptimal protein–protein interface.”
From Defining molecular glues with a dual-nanobody cannabidiol sensor (2022) · cites this paper as [8]
Auxin promotes degradation of a family of transcription repressors by enhancing their otherwise weak interactions with the SCFTIR1 ubiquitin ligase complex.
“auxin promotes the degradation of a family of transcription repressors by enhancing their otherwise weak interactions with the SCFTIR1 ubiquitin ligase complex8.”
From Defining molecular glues with a dual-nanobody cannabidiol sensor (2022) · cites this paper as [8]
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Molecular glue degraders: exciting opportunities for novel drug discovery
Lemaitre, T., Cornu, M., Schwalen, F., Since, M., Kieffer, C., & Voisin-Chiret, A. S. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2306845 · Cited by 36 · see citing works
- Authors
- Calderon-Villalobos, L. I., Tan, X., Zheng, N., & Estelle, M.
- Affiliations
- Brigham and Women's Hospital (US)
- University of Washington (US)
- University of California San Diego (US)
- Corresponding author
- Estelle, M.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-05-26
- Volume
- 2
- Issue
- 7
- Pages
- a005546-a005546
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC2890193
- OpenAlex
- W2161783871
- Cited by
- 177
- References
- 93
- Citations by year
- 2026: 4 · 2025: 11 · 2024: 6 · 2023: 8 · 2022: 7 · 2021: 14 · 2020: 9 · 2019: 11 · 2018: 9 · 2017: 11 · 2016: 7 · 2015: 13 · 2014: 18 · 2013: 17 · 2012: 16
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM043644)
- 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 › Agricultural and Biological Sciences › Plant Science › Plant Parasitism and Resistance
- Keywords
- auxin perception, auxin receptor, TIR1, SCF ubiquitin ligase, Aux/IAA proteins, F-box protein, E3 ubiquitin ligase, transcriptional repression, plant hormone signaling
- MeSH terms
- Hydrolysis, Indoleacetic Acids, Signal Transduction
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