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Mechanism of auxin perception by the TIR1 ubiquitin ligase

Author

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  • Xu Tan

    (University of Washington, School of Medicine, Box 357280, Seattle, Washington 98195, USA)

  • Luz Irina A. Calderon-Villalobos

    (Indiana University, Bloomington, Indiana 47405, USA)

  • Michal Sharon

    (University of Cambridge, Cambridge, CB2 1EW, UK)

  • Changxue Zheng

    (University of Washington, School of Medicine, Box 357280, Seattle, Washington 98195, USA)

  • Carol V. Robinson

    (University of Cambridge, Cambridge, CB2 1EW, UK)

  • Mark Estelle

    (Indiana University, Bloomington, Indiana 47405, USA)

  • Ning Zheng

    (University of Washington, School of Medicine, Box 357280, Seattle, Washington 98195, USA)

Abstract

Auxin is a pivotal plant hormone that controls many aspects of plant growth and development. Perceived by a small family of F-box proteins including transport inhibitor response 1 (TIR1), auxin regulates gene expression by promoting SCF ubiquitin-ligase-catalysed degradation of the Aux/IAA transcription repressors, but how the TIR1 F-box protein senses and becomes activated by auxin remains unclear. Here we present the crystal structures of the Arabidopsis TIR1–ASK1 complex, free and in complexes with three different auxin compounds and an Aux/IAA substrate peptide. These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket. Anchored to the base of the TIR1 pocket, auxin binds to a partially promiscuous site, which can also accommodate various auxin analogues. Docked on top of auxin, the Aux/IAA substrate peptide occupies the rest of the TIR1 pocket and completely encloses the hormone-binding site. By filling in a hydrophobic cavity at the protein interface, auxin enhances the TIR1–substrate interactions by acting as a ‘molecular glue’. Our results establish the first structural model of a plant hormone receptor.

Suggested Citation

  • Xu Tan & Luz Irina A. Calderon-Villalobos & Michal Sharon & Changxue Zheng & Carol V. Robinson & Mark Estelle & Ning Zheng, 2007. "Mechanism of auxin perception by the TIR1 ubiquitin ligase," Nature, Nature, vol. 446(7136), pages 640-645, April.
    • Handle: RePEc:nat:nature:v:446:y:2007:i:7136:d:10.1038_nature05731
    DOI: 10.1038/nature05731
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    Cited by:

    1. Ryan P. Wurz & Huan Rui & Ken Dellamaggiore & Sudipa Ghimire-Rijal & Kaylee Choi & Kate Smither & Albert Amegadzie & Ning Chen & Xiaofen Li & Abhisek Banerjee & Qing Chen & Dane Mohl & Amit Vaish, 2023. "Affinity and cooperativity modulate ternary complex formation to drive targeted protein degradation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Olena S. Tokareva & Kunhua Li & Tara L. Travaline & Ty M. Thomson & Jean-Marie Swiecicki & Mahmoud Moussa & Jessica D. Ramirez & Sean Litchman & Gregory L. Verdine & John H. McGee, 2023. "Recognition and reprogramming of E3 ubiquitin ligase surfaces by α-helical peptides," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    3. Qing Sang & Lusheng Fan & Tianxiang Liu & Yongjian Qiu & Juan Du & Beixin Mo & Meng Chen & Xuemei Chen, 2023. "MicroRNA156 conditions auxin sensitivity to enable growth plasticity in response to environmental changes in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    4. Lingmin Yuan & Fei Gao & Zongyang Lv & Digant Nayak & Anindita Nayak & Priscila dos Santos Bury & Kristin E. Cano & Lijia Jia & Natalia Oleinik & Firdevs Cansu Atilgan & Besim Ogretmen & Katelyn M. Wi, 2022. "Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    5. Jin Liu & Ruth Nussinov, 2009. "The Mechanism of Ubiquitination in the Cullin-RING E3 Ligase Machinery: Conformational Control of Substrate Orientation," PLOS Computational Biology, Public Library of Science, vol. 5(10), pages 1-10, October.
    6. Shiyun Cao & Shoukai Kang & Haibin Mao & Jiayu Yao & Liangcai Gu & Ning Zheng, 2022. "Defining molecular glues with a dual-nanobody cannabidiol sensor," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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