Leucine-Rich Repeat Receptor-Like Kinase1 Is a Key Membrane-Bound Regulator of Abscisic Acid Early Signaling in Arabidopsis

Osakabe, Yuriko; Maruyama, Kyonoshin; Seki, Motoaki; Satou, Masakazu; Shinozaki, Kazuo; Yamaguchi-Shinozaki, Kazuko

doi:10.1105/tpc.104.027474

Cited by 291 publications

(248 citation statements)

References 59 publications

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“…rpk1 mutant showed ABA insensitivity and plants overexpressing RPK1-LRR (including the transmembrane domain) were insensitive to ABA in seedling growth and seed germination, revealing that overexpressed LRR domain has a dominantnegative effect on RPK1 [53]. These studies suggest that extracellular regions of RLKs (serine/threonine receptorlike kinases) play a prominent role in their functions.…”

Section: Msbp1-bak1 Interaction May Play An Important Role In Ligand mentioning

confidence: 91%

Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1

et al. 2009

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Brassinosteroids (BRs) are perceived by transmembrane receptors and play vital roles in plant growth and development, as well as cell in responses to environmental stimuli. The transmembrane receptor BRI1 can directly bind to brassinolide (BL), and BAK1 interacts with BRI1 to enhance the BRI1-mediated BR signaling. Our previous studies indicated that a membrane steroid-binding protein 1 (MSBP1) could bind to BL in vitro and is negatively involved in BR signaling. To further elucidate the underlying mechanism, we here show that MSBP1 specifically interacts with the extracellular domain of BAK1 in vivo in a BL-independent manner. Suppressed cell expansion and BR responses by increased expression of MSBP1 can be recovered by overexpressing BAK1 or its intracellular kinase domain, suggesting that MSBP1 may suppress BR signaling through interacting with BAK1. Subcellular localization studies revealed that both MSBP1 and BAK1 are localized to plasma membrane and endocytic vesicles and MSBP1 accelerates BAK1 endocytosis, which results in suppressed BR signaling by shifting the equilibrium of BAK1 toward endosomes. Indeed, enhanced MSBP1 expression reduces the interaction between BRI1 and BAK1 in vivo, demonstrating that MSBP1 acts as a negative factor at an early step of the BR signaling pathway.

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Section: Msbp1-bak1 Interaction May Play An Important Role In Ligand mentioning

confidence: 91%

Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1

et al. 2009

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“…A leucine-rich repeat receptor-like kinase (LRR-RLK1) appears to be involved in early ABA perception in Arabidopsis (Osakabe and others 2005). These types of plasma-membrane-associated proteins contain an extracellular leucine-rich repeat and a Ser/Thr kinase domain; in many cases, the leucine-rich repeat domain, or the protein complex, functions as a receptor of both peptide and nonpeptide hormones (Osakabe and others 2005 and references therein).…”

Section: Aba Receptionmentioning

confidence: 99%

“…In addition, plant receptor-like kinases may form dimers or tetramers to become active and transduce the ligand-binding signal to downstream cascades. Thus, the isolation and characterization of proteins that are specific partners of the putative receptor are key endeavors, because together they form the ABA signaling complex (Osakabe and others 2005).…”

Section: Aba Receptionmentioning

confidence: 99%

Role of Abscisic Acid in Seed Dormancy

Kermode

2005

J Plant Growth Regul

249

160

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Seed dormancy is an adaptive trait that improves survival of the next generation by optimizing the distribution of germination over time. The agricultural and forest industries rely on seeds that exhibit high rates of germination and vigorous, synchronous growth after germination; hence dormancy is sometimes considered an undesirable trait. The forest industry encounters problems with the pronounced dormancy of some conifer seeds, a feature that can lead to non-uniform germination and poor seedling vigor. In cereal crops, an optimum balance is most sought after; some dormancy at harvest is favored because it prevents germination of the physiologically mature grain in the head prior to harvest (that is, preharvest sprouting), a phenomenon that leads to considerable damage to grain quality and is especially prominent in cool moist environments. The sesquiterpene abscisic acid (ABA) regulates key events during seed formation, such as the deposition of storage reserves, prevention of precocious germination, acquisition of desiccation tolerance, and induction of primary dormancy. Its regulatory role is achieved in part by cross-talk with other hormones and their associated signaling networks, via mechanisms that are largely unknown. Quantitative genetics and functional genomics approaches will contribute to the elucidation of genes and proteins that control seed dormancy and germination, including components of the ABA signal transduction pathway. Dynamic changes in ABA biosynthesis and catabolism elicit hormone-signaling changes that affect downstream gene expression and thereby regulate critical checkpoints at the transitions from dormancy to germination and from germination to growth. Some of the recent developments in these areas are discussed.

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“…Accordingly, FCA appears to be an ABA receptor involved in controlling flowering time but additional ABA receptors must perform ABA perception. Putative candidates might be some plasma membrane receptors, such as RPK1, which is known to be involved in ABA signaling (Osakabe et al, 2005).…”

mentioning

confidence: 99%

Enhancement of Abscisic Acid Sensitivity and Reduction of Water Consumption in Arabidopsis by Combined Inactivation of the Protein Phosphatases Type 2C ABI1 and HAB1

et al. 2006

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Abscisic acid (ABA) plays a key role in plant responses to abiotic stress, particularly drought stress. A wide number of ABAhypersensitive mutants is known, however, only a few of them resist/avoid drought stress. In this work we have generated ABA-hypersensitive drought-avoidant mutants by simultaneous inactivation of two negative regulators of ABA signaling, i.e. the protein phosphatases type 2C (PP2Cs) ABA-INSENSITIVE1 (ABI1) and HYPERSENSITIVE TO ABA1 (HAB1). Two new recessive loss-of-function alleles of ABI1, abi1-2 and abi1-3, were identified in an Arabidopsis (Arabidopsis thaliana) T-DNA collection. These mutants showed enhanced responses to ABA both in seed and vegetative tissues, but only a limited effect on plant drought avoidance. In contrast, generation of double hab1-1 abi1-2 and hab1-1 abi1-3 mutants strongly increased plant responsiveness to ABA. Thus, both hab1-1 abi1-2 and hab1-1 abi1-3 were particularly sensitive to ABA-mediated inhibition of seed germination. Additionally, vegetative responses to ABA were reinforced in the double mutants, which showed a strong hypersensitivity to ABA in growth assays, stomatal closure, and induction of ABA-responsive genes. Transpirational water loss under drought conditions was noticeably reduced in the double mutants as compared to single parental mutants, which resulted in reduced water consumption of whole plants. Taken together, these results reveal cooperative negative regulation of ABA signaling by ABI1 and HAB1 and suggest that fine tuning of ABA signaling can be attained through combined action of PP2Cs. Finally, these results suggest that combined inactivation of specific PP2Cs involved in ABA signaling could provide an approach for improving crop performance under drought stress conditions.

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Leucine-Rich Repeat Receptor-Like Kinase1 Is a Key Membrane-Bound Regulator of Abscisic Acid Early Signaling in Arabidopsis

Cited by 291 publications

References 59 publications

Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1

Membrane steroid-binding protein 1 (MSBP1) negatively regulates brassinosteroid signaling by enhancing the endocytosis of BAK1

Role of Abscisic Acid in Seed Dormancy

Enhancement of Abscisic Acid Sensitivity and Reduction of Water Consumption in Arabidopsis by Combined Inactivation of the Protein Phosphatases Type 2C ABI1 and HAB1

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