Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases

Soon, Fen Fen; Ng, Ley Moy; Zhou, Xiaofeng; West, Graham M.; Kovach, Amanda; Tan, Mingyue; Suino-Powell, Kelly; He, Yuanzheng; Xu, Yong; Chalmers, Michael J.; Brunzelle, J.S.; Zhang, Huiming; Yang, Huaiyu; Jiang, Hualiang; Li, Jun; Yong, Eu Leong; Cutler, Sean R.; Zhu, Jian‐Kang; Griffin, Patrick R.; Melcher, Karsten; Xu, H. Eric

doi:10.1126/science.1215106

Cited by 490 publications

(431 citation statements)

References 34 publications

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“…As shown in Fig. 3f, the structure of HAB1.1 was similar to that described in a previous report 10 . Surprisingly, the predicted structure of HAB1.2 was dramatically changed.…”

Section: Hab1 Undergoes Aba-controlled As During Early Developmentsupporting

confidence: 87%

“…Thus, the immediate question is how this occurs and what the physiological role in plant adaptation is. It is known that in the absence of ABA, the 1:1 interaction of HAB1 and SnRK2.6 switches ABA signalling off 10 . In contrast, the binding of HAB1 by PYLs at the same ratio and in the presence of ABA turns ABA signalling on [5][6][7] .…”

Section: Articlementioning

confidence: 99%

“…ABA binds to PYLs, promoting their interaction with PP2Cs and inhibiting their phosphatase activity [5][6][7] . Thus, SnRK2s are released from PP2C-SnRK2 complexes to phosphorylate downstream effectors and activate ABA signalling 3,5,6,[8][9][10] . Over the past several years, the structures and molecular functions of ABA receptors have received significant attention [9][10][11] .…”

mentioning

confidence: 99%

“…Thus, SnRK2s are released from PP2C-SnRK2 complexes to phosphorylate downstream effectors and activate ABA signalling 3,5,6,[8][9][10] . Over the past several years, the structures and molecular functions of ABA receptors have received significant attention [9][10][11] . PP2Cs are central components of the core PYL-PP2C-SnRK2 regulatory module 1 .…”

mentioning

confidence: 99%

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ABA signalling is fine-tuned by antagonistic HAB1 variants

et al. 2015

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Group A protein type 2C phosphatases (PP2Cs) are negative regulators of abscisic acid (ABA) signalling and plant adaptation to stress. However, our knowledge of the regulation of PP2C activity is limited. Here we report that the PP2C HAB1 undergoes alternative splicing to produce two splice variants, which encode HAB1.1 and HAB1.2, that play opposing roles in ABA-mediated seed germination and ABA-mediated post-germination developmental arrest. HAB1.2 is predominately formed in the presence of ABA and prevents seed germination and post-germinative growth. HAB1.2 interacts with OST1, but cannot inhibit OST1 kinase activity; thus, it functions as a positive regulator of ABA signalling. We also identified an RNA-recognition motif-containing protein, RBM25, as a potential regulator of HAB1 alternative splicing and molecular diversity. Our results reveal a mechanism for turning ABA signalling on and off and for plant adaptation to abiotic stress.

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“…As shown in Fig. 3f, the structure of HAB1.1 was similar to that described in a previous report 10 . Surprisingly, the predicted structure of HAB1.2 was dramatically changed.…”

Section: Hab1 Undergoes Aba-controlled As During Early Developmentsupporting

confidence: 87%

Section: Articlementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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ABA signalling is fine-tuned by antagonistic HAB1 variants

et al. 2015

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“…In Arabidopsis protoplasts, PYR1 and PYLs 1-12 could release ABI1 inhibition of ABA-dependent activation of RD29B-LUC expression by the SnRK2 protein kinases such as OST1/SnRK2.6 [4]. Structural analysis revealed that the interaction between SnRK2.6 and HAB1 mimics the interaction between ABA-bound PYL2 and HAB1 [12]. PYLs can inhibit PP2C activity in the presence of ABA, and thereby activating SnRK2.6, which can phosphorylate slow anion channel1 (SLAC1) and activate SLAC1-mediated ion currents [13,14].…”

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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Characterization of thiol‐based redox modifications of Brassica napusSNF1‐related protein kinase 2.6‐2C

Yoo

Zhang

et al. 2018

FEBS Open Bio

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Sucrose nonfermenting 1‐related protein kinase 2.6 (SnRK2.6), also known as Open Stomata 1 (OST1) in Arabidopsis thaliana, plays a pivotal role in abscisic acid (ABA)‐mediated stomatal closure. Four SnRK2.6 paralogs were identified in the Brassica napus genome in our previous work. Here we studied one of the paralogs, BnSnRK2.6‐2C, which was transcriptionally induced by ABA in guard cells. Recombinant BnSnRK2.6‐2C exhibited autophosphorylation activity and its phosphorylation sites were mapped. The autophosphorylation activity was inhibited by S‐nitrosoglutathione (GSNO) and by oxidized glutathione (GSSG), and the inhibition was reversed by reductants. Using monobromobimane (mBBr) labeling, we demonstrated a dose‐dependent modification of BnSnRK2.6‐2C by GSNO. Furthermore, mass spectrometry analysis revealed previously uncharacterized thiol‐based modifications including glutathionylation and sulfonic acid formation. Of the six cysteine residues in BnSnRK2.6‐2C, C159 was found to have different types of thiol modifications, suggesting its high redox sensitivity and versatility. In addition, mBBr labeling on tyrosine residues was identified. Collectively, these data provide detailed biochemical characterization of redox‐induced modifications and changes of the BnSnRK2.6‐2C activity.

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Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases

Cited by 490 publications

References 34 publications

ABA signalling is fine-tuned by antagonistic HAB1 variants

ABA signalling is fine-tuned by antagonistic HAB1 variants

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

Characterization of thiol‐based redox modifications of Brassica napusSNF1‐related protein kinase 2.6‐2C

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