An LRR receptor kinase controls ABC transporter substrate preferences during plant growth-defense decisions

Aryal, Bibek; Xia, Jian; Hu, Zehan; Stumpe, Michael; Tsering, Tashi; Liu, Jie; Huynh, John; Fukao, Yoichiro; Glöckner, Nina; Huang, Hsin-Yao; Sáncho-Andrés, Gloria; Pakula, Konrad; Ziegler, J.; Gorzolka, Karin; Zwiewka, Marta; Nodzyński, Tomasz; Harter, Klaus; Sánchez-Rodríguez, Clara; Jasiński, Michał; Rosahl, Sabine; Geisler, Markus

doi:10.1016/j.cub.2023.04.029

Cited by 14 publications

(28 citation statements)

References 86 publications

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“…The activity of ABCB19 in auxin export is inhibited by phosphorylation by the photoreceptor kinase PHOTOTROPIN1 ( 52 ). Moreover, it has been shown recently that the substrate preference of some plant ABCB transporters can be switched by phosphorylation provided by an interacting receptor kinase ( 65 ). Further investigations are needed to determine whether ABCB19 is regulated by phosphorylation of its R domain, if so, whether this affects its structural dynamics and substrate specificity, and whether this can explain the additional function of ABCB19 in auxin transport.…”

Section: Discussionmentioning

confidence: 99%

Structure and function of the Arabidopsis ABC transporter ABCB19 in brassinosteroid export

Ying,

Wang,

Wei

et al. 2024

Science

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Brassinosteroids are steroidal phytohormones that regulate plant development and physiology, including adaptation to environmental stresses. Brassinosteroids are synthesized in the cell interior but bind receptors at the cell surface, necessitating a yet to be identified export mechanism. Here, we show that a member of the ATP-binding cassette (ABC) transporter superfamily, ABCB19, functions as a brassinosteroid exporter. We present its structure in both the substrate-unbound and the brassinosteroid-bound states. Bioactive brassinosteroids are potent activators of ABCB19 ATP hydrolysis activity, and transport assays showed that ABCB19 transports brassinosteroids. In Arabidopsis thaliana , ABCB19 and its close homolog, ABCB1, positively regulate brassinosteroid responses. Our results uncover an elusive export mechanism for bioactive brassinosteroids that is tightly coordinated with brassinosteroid signaling.

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Section: Discussionmentioning

confidence: 99%

Structure and function of the Arabidopsis ABC transporter ABCB19 in brassinosteroid export

Ying,

Wang,

Wei

et al. 2024

Science

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“…A physiological consequence of prolonged defense is growth inhibition 16,52 because essential resources are thought to be allocated toward defense 16 . On the molecular level, this coordination of substrate preferences on ABCG36 was shown to be provided by phosphorylation situated in the linker (mainly S825 and S844) repressing IBA export and allowing for CLX export and thus defense 14 . Currently, it is unknown if these phosphorylation events exert an effect on the central binding pocket or extracellular gate, however, this option is not unlikely, as linker phosphorylation-sites and L704 of the extracellular gate are directly connected by the THs of TMD2 (not shown).…”

Section: Discussionmentioning

confidence: 99%

“…Recent work has established the engagement of multiple ABCG36 substrates in different ABCG36-dependent critical, biological processes, including growth and defense 13,14,[29][30][31][32][33][34][35][36] . The abcg36-5 allele uncouples ABCG36 functions in IBAstimulated root growth from ABCG36 activity in extracellular defense 29 but the underlying molecular determinants are unclear.…”

Section: L704f Mutation In Abcg36 Uncouples Export Of Iba and Camalexinmentioning

confidence: 99%

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A key residue of the extracellular gate provides quality control contributing to ABCG substrate specificity

Xia,

Siffert,

Torres

et al. 2024

Preprint

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For G-type ATP-binding cassette (ABC) transporters, a hydrophobic "di-leucine motif" as part of a hydrophobic extracellular gate has been described to separate a large substrate-binding cavity from a smaller upper cavity and proposed to act as a valve controlling drug extrusion. Here, we show that an L704F mutation in the hydrophobic extracellular gate of Arabidopsis ABCG36/PDR8/PEN3 uncouples the export of the auxin precursor indole-3-butyric acid (IBA) from that of the defense compound camalexin (CLX). Molecular dynamics simulations reveal an increase in free energy and pulling forces for CLX at both the entrance and exit sites of ABCG36L704F, respectively, providing a mechanistic rationale for the transport discrimination of CLX. Mutagenesis of L704 to tyrosine allows export of structurally related non-ABCG36 substrates, indole-3-acetic acid (IAA) and indole, suggesting an allosteric communication between the extracellular gate and the central substrate binding pocket. In summary, our work supports the conclusion that L704 is a key residue of the extracellular gate that provides a final quality control contributing to ABCG substrate specificity.

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“…These features were especially prominent in subfamilies LRR‐I, LRR‐III, LRR‐VIII.1, LRR‐VIII.2, LRR‐XI, and LRR‐XII (Figure 1a). These families display both high levels of expansion and between‐species variability, and interestingly they all contain at least one member known to be involved in stress responses (Aryal et al, 2023; Chinchilla et al, 2006; Le et al, 2014; Tang et al, 2015; Uemura et al, 2020; Yeh et al, 2016). The inclusion of additional species in this study did identify expansions, particularly in the LRR‐VIII.1 and LRR‐VIII.2 subfamilies, that were not noted in previous work.…”

Section: Discussionmentioning

confidence: 99%

Differential expansion and retention patterns of LRR‐RLK genes across plant evolution

Kileeg,

Haldar,

Khan

et al. 2023

Plant Direct

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To maximize overall fitness, plants must accurately respond to a host of growth, developmental, and environmental signals throughout their life. Many of these internal and external signals are perceived by the leucine‐rich repeat receptor‐like kinases, which play roles in regulating growth, development, and immunity. This largest family of receptor kinases in plants can be divided into subfamilies based on the conservation of the kinase domain, which demonstrates that shared evolutionary history often indicates shared molecular function. Here we investigate the evolutionary history of this family across the evolution of 112 plant species. We identify lineage‐specific expansions of the malectin‐domain containing subfamily LRR subfamily I primarily in the Brassicales and bryophytes. Most other plant lineages instead show a large expansion in LRR subfamily XII, which in Arabidopsis is known to contain key receptors in pathogen perception. This striking asymmetric expansion may reveal a dichotomy in the evolutionary history and adaptation strategies employed by plants. A greater understanding of the evolutionary pressures and adaptation strategies acting on members of this receptor family offers a way to improve functional predictions for orphan receptors and simplify the identification of novel stress‐related receptors.

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An LRR receptor kinase controls ABC transporter substrate preferences during plant growth-defense decisions

Cited by 14 publications

References 86 publications

Structure and function of the Arabidopsis ABC transporter ABCB19 in brassinosteroid export

Structure and function of the Arabidopsis ABC transporter ABCB19 in brassinosteroid export

A key residue of the extracellular gate provides quality control contributing to ABCG substrate specificity

Differential expansion and retention patterns of LRR‐RLK genes across plant evolution

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