Phosphorylation of the Arabidopsis AtrbohF NADPH oxidase by OST1 protein kinase

Sirichandra, Caroline; Gu, Danan; Hu, Heng-Cheng; Davanture, Marlène; Lee, Sangmee; Djaoui, Michaël; Valot, Benoı̂t; Zivy, Michel; Leung, Jeffrey; Merlot, Sylvain; Kwak, June M.

doi:10.1016/j.febslet.2009.08.033

Cited by 402 publications

(318 citation statements)

References 18 publications

(37 reference statements)

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“…This feedback regulation is achieved by S-nitrosylation of SnRK2.6. ABA-activated SnRK2.6 phosphorylates NADPH oxidases to cause ROS production in guard cells (18,48). The S-nitrosylation of the NADPH oxidase AtRBOHD has been shown to cause inhibition of the NADPH oxidase (28), and thus may also contribute to the NO-mediated negative feedback regulation of ABA signaling.…”

Section: Discussionmentioning

confidence: 99%

Nitric oxide negatively regulates abscisic acid signaling in guard cells by S-nitrosylation of OST1

Wang¹,

Hou³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

315

212

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The phytohormone abscisic acid (ABA) plays important roles in plant development and adaptation to environmental stress. ABA induces the production of nitric oxide (NO) in guard cells, but how NO regulates ABA signaling is not understood. Here, we show that NO negatively regulates ABA signaling in guard cells by inhibiting open stomata 1 (OST1)/sucrose nonfermenting 1 (SNF1)-related protein kinase 2.6 (SnRK2.6) through S-nitrosylation. We found that SnRK2.6 is S-nitrosylated at cysteine 137, a residue adjacent to the kinase catalytic site. Dysfunction in the S-nitrosoglutathione (GSNO) reductase (GSNOR) gene in the gsnor1-3 mutant causes NO overaccumulation in guard cells, constitutive S-nitrosylation of SnRK2.6, and impairment of ABA-induced stomatal closure. Introduction of the Cys137 to Ser mutated SnRK2.6 into the gsnor1-3/ ost1-3 double-mutant partially suppressed the effect of gsnor1-3 on ABA-induced stomatal closure. A cysteine residue corresponding to Cys137 of SnRK2.6 is present in several yeast and human protein kinases and can be S-nitrosylated, suggesting that the S-nitrosylation may be an evolutionarily conserved mechanism for protein kinase regulation.A bscisic acid (ABA) plays critical roles in seed dormancy and germination, plant growth, and adaptation to environmental challenges (1, 2). Stresses, such as drought and high salt conditions, increase ABA concentration in plants as a result of ABA biosynthesis or ABA release from its inactive, conjugated forms (3). In the presence of ABA, the ABA receptors in the PYR1 (Pyrabactin Resistance 1)/PYL (PYR1-Like)/RCAR (Regulatory Component of ABA receptor) protein family bind to and inhibit the activity of clade A protein phosphatase 2Cs (PP2Cs), which are considered as coreceptors and negative regulators of ABA signaling (4-6). This process then results in the release of sucrose nonfermenting 1 (SNF1)-related protein kinase 2s (SnRK2s) from suppression by the PP2Cs. As central components of the ABA signaling pathway, the activated SnRK2s phosphorylate dozens of downstream effectors to regulate various physiological processes, including stomatal closure, root growth and development, seed dormancy, seed germination, and flowering (7).As the gateway for photosynthetic CO 2 uptake and transpirational water loss, stomata are critical for plant growth and physiology (8). ABA regulates stomatal movement and mutations in ABA biosynthesis genes (9), or in the PYL or SnRK2.6 (also known as OST1) genes cause open-stomata phenotypes (10). On the other hand, dysfunction of the PP2Cs or overexpression of RCAR1/PYL9 causes stomatal closure (5). Among the three SnRK2s, SnRK2.2, -2.3, and -2.6, which are most important for ABA signaling, SnRK2.6 is preferentially expressed in guard cells and plays a critical role in stomatal regulation, whereas SnRK2.2 and -2.3 are mainly expressed in seeds and young seedlings and are thus more important for seed germination and seedling growth (4, 11). SnRK2.6 phosphorylates the slow (S-type) anion channel associated 1 and inward potass...

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Section: Discussionmentioning

confidence: 99%

Nitric oxide negatively regulates abscisic acid signaling in guard cells by S-nitrosylation of OST1

Wang¹,

Hou³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

315

212

View full text Add to dashboard Cite

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“…This model allows for other environmental stimuli to further activate AtrbohD/F, for example, by wounding. Interestingly, AtrbohF can be phosphorylated by OST1 (Sirichandra et al, 2009), and AtrbohD has to be phosphorylated to participate in ROS production in response to the elicitor flagellin (Nü hse et al, 2007). It is possible that the integration of signaling from many chloroplasts could occur via the control of AtrbohD/F activation.…”

Section: Systemic Signalingmentioning

confidence: 99%

Oxidative Stress: Antagonistic Signaling for Acclimation or Cell Death?

2010

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Severe environmental stress imposed on plant tissues induces changes in oxygen (O 2 ) metabolism that cause oxidative stress. Oxidative stress occurs when reactive oxygen species (ROS) are not rapidly scavenged and the rate of repair of damaged cell components fails to keep pace with the rate of damage. If this situation persists, irreversible damage results in a loss of physiological competence and eventual cell death. However, ROS production in leaves resulting from moderate environmental stresses, within the adaptive range of the plant, also has important local and systemic signaling roles. In these circumstances, ROS production induces defense mechanisms that protect the plant but do not result in oxidative stress. We shall illustrate ROS involvement in signaling in both of these situations by considering the role of chloroplasts in initiating cellular responses to environmental perturbations, choosing examples where this organelle interacts with specific signaling pathways.

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“…Activated SnRK2.2/2.3/2.6 can phosphorylate and activate transcription factors such as ABFs/ AREBs [20,21] to induce the expression of ABAresponsive genes such as RD29B [4]. In guard cells, the SnRK2s can also phosphorylate and activate the NADPH oxidase catalytic subunit RBOHF, leading to the production of reactive oxygen species (ROS) [17,22,23]. SnRK2s also interact with and phosphorylate plasma membrane anion channels such as SLAC1 to regulate ion transport [13,[24][25][26].…”

Section: Introductionmentioning

confidence: 99%

The unique mode of action of a divergent member of the ABA-receptor protein family in ABA and stress signaling

et al. 2013

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Proteins in the PYR/PYL/RCAR family (PYLs) are known as receptors for the phytohormone ABA. Upon ABA binding, PYL adopts a conformation that allows it to interact with and inhibit clade A protein phosphatase 2Cs (PP2Cs), which are known as the co-receptors for ABA. Inhibition of the PP2Cs then leads to the activation of the SnRK2 family protein kinases that phosphorylate and activate downstream effectors in ABA response pathways. The PYL family has 14 members in Arabidopsis, 13 of which have been demonstrated to function as ABA receptors. The function of PYL13, a divergent member of the family, has been enigmatic. We report here that PYL13 differs from the other PYLs in three key residues that affect ABA perception, and mutations in these three residues can convert PYL13 into a partially functional ABA receptor. Transgenic plants overexpressing PYL13 show increased ABA sensitivity in seed germination and postgermination seedling establishment as well as decreased stomatal conductance, increased water-use efficiency, accelerated stress-responsive gene expression, and enhanced drought resistance. pyl13 mutant plants are less sensitive to ABA inhibition of postgermination seedling establishment. PYL13 interacts with and inhibits some members of clade A PP2Cs (PP2CA in particular) in an ABA-independent manner. PYL13 also interacts with the other PYLs and antagonizes their function as ABA receptors. Our results show that PYL13 is not an ABA receptor but can modulate the ABA pathway by interacting with and inhibiting both the PYL receptors and the PP2C co-receptors.

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Phosphorylation of the Arabidopsis AtrbohF NADPH oxidase by OST1 protein kinase

Cited by 402 publications

References 18 publications

Nitric oxide negatively regulates abscisic acid signaling in guard cells by S-nitrosylation of OST1

Nitric oxide negatively regulates abscisic acid signaling in guard cells by S-nitrosylation of OST1

Oxidative Stress: Antagonistic Signaling for Acclimation or Cell Death?

The unique mode of action of a divergent member of the ABA-receptor protein family in ABA and stress signaling

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