Functional analysis in Arabidopsis of FsPTP1, a tyrosine phosphatase from beechnuts, reveals its role as a negative regulator of ABA signaling and seed dormancy and suggests its involvement in ethylene signaling modulation

Alonso-Ramírez, Ana; Rodrı́guez, Dolores; Reyes, David; Jiménez, Jesús Ángel; Nicolás, G.; Nicolás, Carlos

doi:10.1007/s00425-011-1426-8

Cited by 6 publications

(3 citation statements)

References 46 publications

(69 reference statements)

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“…In addition, overexpression in Arabidopsis seeds of a beechnut tyrosine phosphatase, FsPTP1 , reduces dormancy, through both ABA signaling down-regulation and EIN2 up-regulation, suggesting that the negative role of FsPTP1 in ABA signaling might result from modulation of C 2 H 4 signaling (Alonso-Ramirez et al, 2011). This central role of EIN2 in mediating cross-links between hormonal response pathways has also been reported in plant response to abiotic and biotic stresses (Wang et al, 2007).…”

Section: Ethylene Biosynthesis Signaling and Aba Crosstalk In Seed mentioning

confidence: 99%

ABA crosstalk with ethylene and nitric oxide in seed dormancy and germination

Arc¹,

Sechet²,

Corbineau³

et al. 2013

Front. Plant Sci.

208

234

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Dormancy is an adaptive trait that enables seed germination to coincide with favorable environmental conditions. It has been clearly demonstrated that dormancy is induced by abscisic acid (ABA) during seed development on the mother plant. After seed dispersal, germination is preceded by a decline in ABA in imbibed seeds, which results from ABA catabolism through 8′-hydroxylation. The hormonal balance between ABA and gibberellins (GAs) has been shown to act as an integrator of environmental cues to maintain dormancy or activate germination. The interplay of ABA with other endogenous signals is however less documented. In numerous species, ethylene counteracts ABA signaling pathways and induces germination. In Brassicaceae seeds, ethylene prevents the inhibitory effects of ABA on endosperm cap weakening, thereby facilitating endosperm rupture and radicle emergence. Moreover, enhanced seed dormancy in Arabidopsis ethylene-insensitive mutants results from greater ABA sensitivity. Conversely, ABA limits ethylene action by down-regulating its biosynthesis. Nitric oxide (NO) has been proposed as a common actor in the ABA and ethylene crosstalk in seed. Indeed, convergent evidence indicates that NO is produced rapidly after seed imbibition and promotes germination by inducing the expression of the ABA 8′-hydroxylase gene, CYP707A2, and stimulating ethylene production. The role of NO and other nitrogen-containing compounds, such as nitrate, in seed dormancy breakage and germination stimulation has been reported in several species. This review will describe our current knowledge of ABA crosstalk with ethylene and NO, both volatile compounds that have been shown to counteract ABA action in seeds and to improve dormancy release and germination.

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Section: Ethylene Biosynthesis Signaling and Aba Crosstalk In Seed mentioning

confidence: 99%

ABA crosstalk with ethylene and nitric oxide in seed dormancy and germination

Arc¹,

Sechet²,

Corbineau³

et al. 2013

Front. Plant Sci.

208

234

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“…1 ) [ 83 ]. Additionally, Yoo et al (2008) have reported the role of MKK9-MPK3/MPK6 cascade in the regulation of ethylene-insensitive3 ( EIN3 )-mediated transcription in ethylene signaling and shown to act downstream of the ethylene receptors [ 84 ].…”

Section: Functional Role Of Protein Tyr Phosphorylation and Dsp In Plmentioning

confidence: 99%

Role of Protein Tyrosine Phosphatases in Plants

Shankar

Agrawal

Sharma

et al. 2015

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Reversible protein phosphorylation is a crucial regulatory mechanism that controls many biological processes in eukaryotes. In plants, phosphorylation events primarily occur on serine (Ser) and threonine (Thr) residues, while in certain cases, it was also discovered on tyrosine (Tyr) residues. In contrary to plants, extensive reports on Tyr phosphorylation regulating a large numbers of biological processes exist in animals. Despite of such prodigious function in animals, Tyr phosphorylation is a least studied mechanism of protein regulation in plants. Recently, various chemical analytical procedures have strengthened the view that Tyr phosphorylation is equally prevalent in plants as in animals. However, regardless of Tyr phosphorylation events occuring in plants, no evidence could be found for the existence of gene encoding for Tyr phosphorylation i.e. the typical Tyr kinases. Various methodologies have suggested that plant responses to stress signals and developmental processes involved modifications in protein Tyr phosphorylation. Correspondingly, various reports have established the role of PTPs (Protein Tyrosine Phosphatases) in the dephosphorylation and inactivation of mitogen activated protein kinases (MAPKs) hence, in the regulation of MAPK signaling cascade. Besides this, many dual specificity protein phosphatases (DSPs) are also known to bind starch and regulate starch metabolism through reversible phosphorylation. Here, we are emphasizing the significant progress on protein Tyr phosphatases to understand the role of these enzymes in the regulation of post-translational modification in plant physiology and development.

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“…AtPTP1 has been shown to bind to and dephosphorylate MPK3/MPK6 and to play a positive role in the response of cells to salt stress‐induced microtubule depolymerization (Zhou, Chen, Sun, & Li, 2017). Similarly, the closest homolog of AtPTP1 from Fagus sylvatica , FsPTP1 , produced salt resistance when ectopically expressed in Arabidopsis (Alonso‐Ramirez et al, 2011). Members of another subclass of DsPTPs, the PFA‐DSP group, were shown to be involved in pathogen and drought stress responses in rice and Arabidopsis (He et al, 2012; Liu et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

AtPFA‐DSP3, an atypical dual‐specificity protein tyrosine phosphatase, affects salt stress response by modulating MPK3 and MPK6 activity

Xin

Ning

et al. 2021

Plant Cell & Environment

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Protein phosphorylation, especially serine/threonine and tyrosine phosphorylation, plays significant roles in signalling during plant growth and development as well as plant responses to biotic or abiotic stresses. Dual-specificity protein tyrosine phosphatases dephosphorylate components of these signalling pathways. Here, we report that an atypical dual-specificity protein tyrosine phosphatase, AtPFA-DSP3 (DSP3), negatively affects the response of plants to high-salt conditions. A DSP3 loss-offunction mutant showed reduced sensitivity to salt treatment. DSP3 was primarily localized in nuclei and was degraded during salt treatment. Compared to wild type, the level of ROS was lower in the dsp3 mutant and higher in plants ectopically expressing DSP3, indicating that higher DSP3 level was associated with increased ROS production. DSP3 interacted with and dephosphorylated MPK3 and MPK6.Genetic analyses of a dsp3mpk3 double mutant revealed that DSP3's effect on salt stress depends on MPK3. Moreover, the phosphatase activity of DSP3 was required for its role in salt signalling. These results indicate that DSP3 is a negative regulator of salt responses in Arabidopsis by directly modulating the accumulation of phosphorylated MPK3 and MPK6.

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Functional analysis in Arabidopsis of FsPTP1, a tyrosine phosphatase from beechnuts, reveals its role as a negative regulator of ABA signaling and seed dormancy and suggests its involvement in ethylene signaling modulation

Cited by 6 publications

References 46 publications

ABA crosstalk with ethylene and nitric oxide in seed dormancy and germination

ABA crosstalk with ethylene and nitric oxide in seed dormancy and germination

Role of Protein Tyrosine Phosphatases in Plants

AtPFA‐DSP3, an atypical dual‐specificity protein tyrosine phosphatase, affects salt stress response by modulating MPK3 and MPK6 activity

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