A protein phosphatase 2C, AP2C1, interacts with and negatively regulates the function of CIPK9 under potassium-deficient conditions in Arabidopsis

Singh, Amarjeet; Yadav, Akhilesh Kumar; Kaur, Kanwaljeet; Sanyal, Sibaji K.; Jha, Saroj Kumar; Fernandes, Joel Lars; Sharma, Pankhuri; Tokas, Indu; Pandey, Amita; Luan, Sheng; Pandey, Girdhar K.

doi:10.1093/jxb/ery182

Cited by 69 publications

(36 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AtCIPK24 associates with the PP2C ABI2 (ABA insensitive 2) to regulate resistance to salt and ABA [63]. AtCIPK9 interacts with AP2C1 (AKT1-interacting PP2C 1) under potassium-deficient conditions in Arabidopsis [76]. The PPI motif negatively influences the function of the NAF motif [70].…”

Section: Mechanisms Of the Cbl-cipk Modulementioning

confidence: 99%

“…As a PP2C protein family member, AIP1 interacts with AtCIPK23, and both interact with AKT1 to modify its activity by phosphorylation and dephosphorylation [153]. A recent study has reported that the 2C-type phosphatase protein AP2C1 interacts with AtCIPK9 in the cytoplasm and dephosphorylates the autophosphorylated AtCIPK9 to regulate K + -deficiency responses [76]. Moreover, another K + channel, AKT2, has been found to regulate the CBL-CIPK complex.…”

Section: Nutrient Deficiency In Plantsmentioning

confidence: 99%

See 1 more Smart Citation

The CBL–CIPK Pathway in Plant Response to Stress Signals

et al. 2020

IJMS

View full text Add to dashboard Cite

Plants need to cope with multitudes of stimuli throughout their lifecycles in their complex environments. Calcium acts as a ubiquitous secondary messenger in response to numerous stresses and developmental processes in plants. The major Ca2+ sensors, calcineurin B-like proteins (CBLs), interact with CBL-interacting protein kinases (CIPKs) to form a CBL–CIPK signaling network, which functions as a key component in the regulation of multiple stimuli or signals in plants. In this review, we describe the conserved structure of CBLs and CIPKs, characterize the features of classification and localization, draw conclusions about the currently known mechanisms, with a focus on novel findings in response to multiple stresses, and summarize the physiological functions of the CBL–CIPK network. Moreover, based on the gradually clarified mechanisms of the CBL–CIPK complex, we discuss the present limitations and potential prospects for future research. These aspects may provide a deeper understanding and functional characterization of the CBL–CIPK pathway and other signaling pathways under different stresses, which could promote crop yield improvement via biotechnological intervention.

show abstract

Section: Mechanisms Of the Cbl-cipk Modulementioning

confidence: 99%

Section: Nutrient Deficiency In Plantsmentioning

confidence: 99%

The CBL–CIPK Pathway in Plant Response to Stress Signals

et al. 2020

IJMS

View full text Add to dashboard Cite

show abstract

“…ABI1 could also directly dephosphorylate SLAC1 (Brandt et al, ). Clade A and Clade B PP2Cs also regulate CIPK9 (Singh et al, ), CIPK23 (Lee et al, ; Léran et al, ), and CIPK6 (Lan, Lee, Che, Jiang, & Luan, ). PP2C regulation of Ca2+/calmodulin‐dependent protein kinase has been observed in rice (Ni et al, ; Shi et al, ).…”

Section: Mechanisms To Decrease the Level Of Protein Phosphorylationmentioning

confidence: 99%

“…AP2C1 dephosphorylation of MAPK4 and MAPK6 is also important in plant innate immunity signalling (Schweighofer et al, ; Shubchynskyy et al, ). AP2C1 also interacted with and dephosphorylated CIPK9 to regulate potassium deficiency responses (Singh et al, ) and may regulate nematode resistance (Sidonskaya et al, ).…”

Section: Pp2cs the Largest Group Of Plant Protein Phosphatasesmentioning

confidence: 99%

The flip side of phospho‐signalling: Regulation of protein dephosphorylation and the protein phosphatase 2Cs

Bhaskara

Wong

Verslues

2019

Plant Cell & Environment

View full text Add to dashboard Cite

Protein phosphorylation is a key signalling mechanism and has myriad effects on protein function. Phosphorylation by protein kinases can be reversed by protein phosphatases, thus allowing dynamic control of protein phosphorylation. Although this may suggest a straightforward kinase-phosphatase relationship, plant genomes contain five times more kinases than phosphatases. Here, we examine phospho-signalling from a protein phosphatase centred perspective and ask how relatively few phosphatases regulate many phosphorylation sites. The most abundant class of plant phosphatases, the protein phosphatase 2Cs (PP2Cs), is surrounded by a web of regulation including inhibitor and activator proteins as well as posttranslational modifications that regulate phosphatase activity, control phosphatase stability, or determine the subcellular locations where the phosphatase is present and active. These mechanisms are best established for the Clade A PP2Cs, which are key components of stress and abscisic acid signalling.We also describe other PP2C clades and illustrate how these phosphatases are highly regulated and involved in a wide range of physiological functions. Together, these examples of multiple layers of phosphatase regulation help explain the unbalanced kinase-phosphatase ratio. Continued use of phosphoproteomics to examine phosphatase targets and phosphatase-kinase relationships will be important for deeper understanding of phosphoproteome regulation.

show abstract

“…Another CBL member, CBL10, is capable of CIPK-independent negative regulation of AKT1 activity, suggesting a role in maintaining balance of K + uptake (Ren et al, 2013). CIPK9, most likely paired with CBL2 or CBL3, also regulates K + homeostasis under low K + conditions via phosphorylation of a yet unknown target (Pandey et al, 2007a;Liu et al, 2012b;Singh et al, 2018). In addition, members of the cyclic-nucleotide gated channel family CNGC3, CNGC10, and CNGC13 (Kaplan et al, 2007;Caballero et al, 2012;Ragel et al, 2019), and the cationproton antiporter CHX13 (Zhao et al, 2008) have also been reported to mediate K + flux into root cell.…”

Section: Calcium-dependent Import Of Potassium and Anions-regulator Omentioning

confidence: 99%

Calcium-Regulated Phosphorylation Systems Controlling Uptake and Balance of Plant Nutrients

Saito

Uozumi

2020

Front. Plant Sci.

View full text Add to dashboard Cite

Essential elements taken up from the soil and distributed throughout the whole plant play diverse roles in different tissues. Cations and anions contribute to maintenance of intracellular osmolarity and the formation of membrane potential, while nitrate, ammonium, and sulfate are incorporated into amino acids and other organic compounds. In contrast to these ion species, calcium concentrations are usually kept low in the cytosol and calcium displays unique behavior as a cytosolic signaling molecule. Various environmental stresses stimulate increases in the cytosolic calcium concentration, leading to activation of calcium-regulated protein kinases and downstream signaling pathways. In this review, we summarize the stress responsive regulation of nutrient uptake and balancing by two types of calcium-regulated phosphorylation systems: CPK and CBL-CIPK. CPK is a family of protein kinases activated by calcium. CBL is a group of calcium sensor proteins that interact with CIPK kinases, which phosphorylate their downstream targets. In Arabidopsis, quite a few ion transport systems are regulated by CPKs or CBL-CIPK complexes, including channels/transporters that mediate transport of potassium (

show abstract

A protein phosphatase 2C, AP2C1, interacts with and negatively regulates the function of CIPK9 under potassium-deficient conditions in Arabidopsis

Abstract: AP2C1 dephosphorylates CIPK9 to negatively regulate its function in controlling root growth and seedling development under low-K+ conditions in Arabidopsis.

Cited by 69 publications

References 55 publications

The CBL–CIPK Pathway in Plant Response to Stress Signals

The CBL–CIPK Pathway in Plant Response to Stress Signals

The flip side of phospho‐signalling: Regulation of protein dephosphorylation and the protein phosphatase 2Cs

Calcium-Regulated Phosphorylation Systems Controlling Uptake and Balance of Plant Nutrients

Contact Info

Product

Resources

About