Biochemical characterization of the tomato phosphatidylinositol-specific phospholipase C (PI-PLC) family and its role in plant immunity

Abd-El-Haliem, Ahmed; Vossen, Jack H.; Zeijl, Arjan van; Dezhsetan, Sara; Testerink, Christa; Seidl, Michael; Beck, Martina; Strutt, James; Robatzek, Silke; Joosten, M.H.A.J.

doi:10.1016/j.bbalip.2016.01.017

Cited by 30 publications

(32 citation statements)

References 87 publications

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“…PI‐PLC substrates, in the order of preference as previously reported following in vitro studies, are PIP 2 , phosphatidylinositol‐4‐phosphate (PI4P) and phosphatidylinositol (PI) (Ellis et al ; Kopka et al ; Mueller‐Roeber and Pical ; Meijer and Munnik ; Abd‐El‐Haliem et al ). In plants, PI is the most abundant compound, followed by PI4P and PIP 2 (Munnik and Zarza ).…”

Section: Pi‐plc Substrates In Cell Membranesmentioning

confidence: 84%

“…This indicates that PI‐PLCs could have been subjected to multiple duplication rounds, before the divergence between monocots and dicots and after which monocots lost PI‐PLCs multiple times. Another explanation could be that the duplications are dicot‐specific, while the sequences in the SlPLC4 group remained conserved (Abd‐El‐Haliem et al ).…”

Section: Domain Structure and Phylogeny Of Eukaryotic Pi‐plcsmentioning

confidence: 99%

“…Likewise, PI cannot be excluded from acting as a PI‐PLC substrate during signaling under specific conditions as it exists in relatively high amounts in plants, when compared to PI4P and PIP 2 (Munnik and Zarza ). In vitro PI hydrolysis by PI‐PLC requires higher Ca 2+ levels (Kopka et al ; Abd‐El‐Haliem et al ), suggesting that it might be secondarily used as a PI‐PLC substrate in vivo , at a later stage after immune receptor activation when the Ca 2+ levels peak.…”

Section: Pi‐plc Substrates In Cell Membranesmentioning

confidence: 99%

“…Moreover, elicitor treatment of suspension‐cultured soybean ( Glycine max ) cells led to a reduction of the PI4P and PIP 2 levels, indicating PI‐PLC activation (Legendre et al ). Inhibition of PI‐PLC activity by the PI‐PLC inhibitor U73122 in cotyledons of Arabidopsis seedlings treated with the flagellin‐derived peptide flg22, suppressed effector‐mediated endocytosis of the matching receptor‐like kinase (RLK) flagellin sensing 2 (FLS2), and blocked immune responses (Abd‐El‐Haliem et al ). Furthermore, pretreatment with U73122 also suppressed the proton influx that is induced by flg22 in tobacco suspension‐cultured cells, as determined by an attenuation of the medium alkalization response (Abd‐El‐Haliem et al ).…”

Section: Pi‐plc Substrates Modulate the Activity Of Signaling Proteinmentioning

confidence: 99%

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Plant phosphatidylinositol‐specific phospholipase C at the center of plant innate immunity

Abd-El-Haliem

Joosten

2017

JIPB

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Understanding plant resistance to pathogenic microbes requires detailed information on the molecular mechanisms controlling the execution of plant innate immune responses. A growing body of evidence places phosphoinositide-specific phospholipase C (PI-PLC) enzymes immediately downstream of activated immune receptors, well upstream of the initiation of early defense responses. An increase of the cytoplasmic levels of free Ca 2þ , lowering of the intercellular pH and the oxidative burst are a few examples of such responses and these are regulated by PI-PLCs. Consequently, PI-PLC activation represents an early primary signaling switch between elicitation and response involving the controlled hydrolysis of essential signaling phospholipids, thereby simultaneously generating lipid and non-lipid second messenger molecules required for a swift cellular defense response. Here, we elaborate on the signals generated by PI-PLCs and their respective downstream effects, while providing an inventory of different types of evidence describing the involvement of PI-PLCs in various aspects of plant immunity. We project the discussed information into a model describing the cellular events occurring after the activation of plant immune receptors. With this review we aim to provide new insights supporting future research on plant PI-PLCs and the development of plants with improved resistance.

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Section: Pi‐plc Substrates In Cell Membranesmentioning

confidence: 84%

Section: Domain Structure and Phylogeny Of Eukaryotic Pi‐plcsmentioning

confidence: 99%

Section: Pi‐plc Substrates In Cell Membranesmentioning

confidence: 99%

Section: Pi‐plc Substrates Modulate the Activity Of Signaling Proteinmentioning

confidence: 99%

See 2 more Smart Citations

Plant phosphatidylinositol‐specific phospholipase C at the center of plant innate immunity

Abd-El-Haliem

Joosten

2017

JIPB

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“…Recombinant soybean and tomato PI‐PLC proteins also show higher activities towards both PtdIns4P and PtdIns(4,5)P 2 (Shi et al ., ; Abd‐El‐Haliem et al ., ). In Arabidopsis , knockout of AtPLC2 significantly increased concentrations of PtdIns4P and PtdIns(4,5)P 2 (Kanehara et al ., ).…”

Section: Discussionmentioning

confidence: 99%

A phosphoinositide‐specific phospholipase C pathway elicits stress‐induced Ca²⁺ signals and confers salt tolerance to rice

Wang

Yan

et al. 2017

New Phytologist

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In animal cells, phospholipase C (PLC) isoforms predominantly hydrolyze phosphatidylinositol-4,5-biphosphates [PtdIns(4,5)P ] into the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate [Ins(1,4,5)P ] to regulate diverse biological processes. By contrast, the molecular mechanisms and physiological significance of PLC signaling in plants still awaits full elucidation. Here, we identified a rice (Oryza sativa cv) PI-PLC, OsPLC1, which preferred to hydrolyze phosphatidylinositol-4-phosphate (PtdIns4P) and elicited stress-induced Ca signals regulating salt tolerance. Analysis by ion chromatography revealed that the concentration of PtdIns4P was c. 28 times of that of PtdIns(4,5)P in shoots. OsPLC1 not only converted PtdIns(4,5)P but also - and even more efficiently - converted PtdIns4P into DAG and Ins(1,4,5)P in vitro and in vivo. Salt stress induced the recruitment of OsPLC1 from cytoplasm to plasma membrane, where it hydrolyzed PtdIns4P. The stress-induced Ca signaling was dependent on OsPLC1, and the PLC-mediated Ca signaling was essential for controlling Na accumulation in leaf blades, thus establishing whole plant salt tolerance. Our work identifies a conversion pathway and physiological function for PtdIns4P pools in rice and reveals the connection between phosphoinositides and Ca signals mediated by PLC during salt stress responses.

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The effect of plant stress on phosphoinositides

Morales-Morales

González-Kantún

Rodríguez-Zapata

et al. 2019

Cell Biochemistry & Function

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Phosphoinositides are very versatile molecules with a plethora of functions such as cytokinesis, chemotaxis, cell survival, and cell death. Their functions depend on the proteins with which they interact. Thus, when interacting with phospholipases, phosphatases, or kinases, they can be precursors of second messengers in different signalling pathways. They could be second messengers themselves and interact directly with other proteins to modulate their functions trough changing its localization and activity or enhancing its synthesis rate. Because they are more abundant in animal cells and their importance in diseases such as cancer has taken priority, the study of the phosphoinositides in plants has not evolved to the same extent. Nevertheless, several studies have shown the significance of these lipids in plant cells viability and environmental response. This review focuses on phosphoinositides response to abiotic and biotic stress, showing their implication in plant survival during different stages of development.Significance of the studyThis review is focused on plant PIPs functions in stress, highlighting in the main differences between plant and mammal PIPs and the novel interactions that could be extrapolated to animal models to contribute in a better understanding of these pivotal molecules.

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Biochemical characterization of the tomato phosphatidylinositol-specific phospholipase C (PI-PLC) family and its role in plant immunity

Cited by 30 publications

References 87 publications

Plant phosphatidylinositol‐specific phospholipase C at the center of plant innate immunity

Plant phosphatidylinositol‐specific phospholipase C at the center of plant innate immunity

A phosphoinositide‐specific phospholipase C pathway elicits stress‐induced Ca²⁺ signals and confers salt tolerance to rice

The effect of plant stress on phosphoinositides

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Biochemical characterization of the tomato phosphatidylinositol-specific phospholipase C (PI-PLC) family and its role in plant immunity

Cited by 30 publications

References 87 publications

Plant phosphatidylinositol‐specific phospholipase C at the center of plant innate immunity

Plant phosphatidylinositol‐specific phospholipase C at the center of plant innate immunity

A phosphoinositide‐specific phospholipase C pathway elicits stress‐induced Ca2+ signals and confers salt tolerance to rice

The effect of plant stress on phosphoinositides

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A phosphoinositide‐specific phospholipase C pathway elicits stress‐induced Ca²⁺ signals and confers salt tolerance to rice