A Plant 126-kDa Phosphatidylinositol 4-Kinase with a Novel Repeat Structure

Hou, Xue; Pical, Christophe; Brearley, Charles A.; Elge, Stephan; Müller‐Röber, Bernd

doi:10.1074/jbc.274.9.5738

Cited by 67 publications

(16 citation statements)

References 59 publications

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“…Although PI4K activity was found in plants many years ago, the isolation and functional analysis of a full-length plant PI4K cDNA was first reported in 1999 (Xue et al , 1999). AtPI4Kβ was the first PI4K cloned from a plant, and its transcript levels were similar in all tissues.…”

Section: Introductionmentioning

confidence: 99%

“…AtPI4Kβ was the first PI4K cloned from a plant, and its transcript levels were similar in all tissues. Treatment of seedlings with hormones, CaCl 2 , or NaCl had no effect on AtPI4Kβ mRNA levels (Xue et al , 1999). Currently, eight Arabidopsis putative type II PI4Ks, four Arabidopsis putative type III PI4Ks, and two cotton putative type II PI4Ks are reported (Mueller-Roeber and Pical, 2002; Galvão et al , 2008; Liu et al , 2012).…”

Section: Introductionmentioning

confidence: 99%

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A wheat PI4K gene whose product possesses threonine autophophorylation activity confers tolerance to drought and salt in Arabidopsis

Liu

et al. 2013

Journal of Experimental Botany

102

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Phosphoinositides are involved in regulation of recruitment and activity of signalling proteins in cell membranes. Phosphatidylinositol (PI) 4-kinases (PI4Ks) generate PI4-phosphate the precursor of regulatory phosphoinositides. No type II PI4K research on the abiotic stress response has previously been reported in plants. A stress-inducible type II PI4K gene, named TaPI4KIIγ, was obtained by de novo transcriptome sequencing of drought-treated wheat (Triticum aestivum). TaPI4KIIγ, localized on the plasma membrane, underwent threonine autophosphorylation, but had no detectable lipid kinase activity. Interaction of TaPI4KIIγ with wheat ubiquitin fusion degradation protein (TaUDF1) indicated that it might be hydrolysed by the proteinase system. Overexpression of TaPI4KIIγ revealed that it could enhance drought and salt stress tolerance during seed germination and seedling growth. A ubdkγ7 mutant, identified as an orthologue of TaPI4KIIγ in Arabidopsis, was sensitive to salt, polyethylene glycol (PEG), and abscisic acid (ABA), and overexpression of TaPI4KIIγ in the ubdkγ7 mutant compensated stress sensitivity. TaPI4KIIγ promoted root growth in Arabidopsis, suggesting that TaPI4KIIγ might enhance stress resistance by improving root growth. Overexpression of TaPI4KIIγ led to an altered expression level of stress-related genes and changes in several physiological traits that made the plants more tolerant to stress. The results provided evidence that overexpression of TaPI4KIIγ could improve drought and salt tolerance.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A wheat PI4K gene whose product possesses threonine autophophorylation activity confers tolerance to drought and salt in Arabidopsis

Liu

et al. 2013

Journal of Experimental Botany

102

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“…Another motif of unknown function, situated in the central part of the Pik1 primary structure and dubbed the novel homology domain (NHD), is a specific hallmark of Type IIIβ PtdIns 4-kinases ( Figure 3B). Stt4, by contrast, possesses an apparent PH domain sandwiched between its LKU and catalytic domains, a diagnostic feature of Type IIIα PtdIns 4-kinases ( Figure 3B) [213][214][215].…”

Section: 22mentioning

confidence: 99%

Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae

Strahl

Thorner

2007

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

274

315

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It is now well appreciated that derivatives of phosphatidylinositol (PtdIns) are key regulators of many cellular processes in eukaryotes. Of particular interest are phosphoinositides (mono-and polyphosphorylated adducts to the inositol ring in PtdIns), which are located at the cytoplasmic face of cellular membranes. Phosphoinositides serve both a structural and a signaling role via their recruitment of proteins that contain phosphoinositide-binding domains. Phosphoinositides also have a role as precursors of several types of second messengers for certain intracellular signaling pathways. Realization of the importance of phosphoinositides has brought increased attention to characterization of the enzymes that regulate their synthesis, interconversion, and turnover. Here we review the current state of our knowledge about the properties and regulation of the ATP-dependent lipid kinases responsible for synthesis of phosphoinositides and also the additional temporal and spatial controls exerted by the phosphatases and a phospholipase that act on phosphoinositides in yeast.

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“…7). DISCUSSION The strongest evidence that a phosphoinositide/Ca 2ϩ signal transduction system operates in plant cells has been provided by the identification of homologues of the components of the classical animal phosphoinositide system, such as phosphoinositide-metabolizing enzymes (22,23,25,26,28) and inositol lipids themselves (19,21,38,45,46). In the present study, we have identified phosphoinositides as well as other phospholipids in suspension-cultured A. thaliana cells, and provide evidence that some of these lipids may play an important function in the response to salt stress, and hyperosmotic stress.…”

Section: Effect Of Salt and Hyperosmotic Stresses Onmentioning

confidence: 99%

“…cDNA clones representing functional enzymes necessary for the synthesis of these phospholipids, phosphatidylinositol (PtdIns) 4-kinase (22), phosphatidylinositol monophosphate (PtdInsP) kinase (23), PtdIns 3-kinase (24), have also been characterized in plants. Several PI-PLC isoforms have been cloned from plant species (25)(26)(27)(28).…”

mentioning

confidence: 99%

Salinity and Hyperosmotic Stress Induce Rapid Increases in Phosphatidylinositol 4,5-Bisphosphate, Diacylglycerol Pyrophosphate, and Phosphatidylcholine in Arabidopsis thaliana Cells

Pical¹,

Westergren²,

Dove³

et al. 1999

Journal of Biological Chemistry

Self Cite

187

178

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In animal cells, phosphoinositides are key components of the inositol 1,4,5-trisphosphate/diacylglycerolbased signaling pathway, but also have many other cellular functions. These lipids are also believed to fulfill similar functions in plant cells, although many details concerning the components of a plant phosphoinositide system, and their regulation are still missing. Only recently have the different phosphoinositide isomers been unambiguously identified in plant cells. Another problem that hinders the study of the function of phosphoinositides and their derivatives, as well as the regulation of their metabolism, in plant cells is the need for a homogenous, easily obtainable material, from which the extraction and purification of phospholipids is relatively easy and quantitatively reproducible. We present here a thorough characterization of the phospholipids purified from [ 32 P]orthophosphate-and myo-[2-3 H]inositol-radiolabeled Arabidopsis thaliana suspension-cultured cells. We then show that NaCl treatment induces dramatic increases in the levels of phosphatidylinositol 4,5-bisphosphate and diacylglycerol pyrophosphate and also affects the turnover of phosphatidylcholine. The increase in phosphatidylinositol 4,5-bisphosphate was also observed with a non-ionic hyperosmotic shock. In contrast, the increase in diacylglycerol pyrophosphate and the turnover of phosphatidylcholine were relatively specific to salt treatments as only minor changes in the metabolism of these two phospholipids were detected when the cells were treated with sorbitol instead of NaCl.Phosphoinositides are quantitatively minor phospholipids that play an important role in the transduction of physiological signals, such as hormones, growth factors, and neurotransmitters in animal cells (1). One of the key early events triggered by these physiological stimuli is the activation of phosphoinositide-specific phospholipase C (PI-PLC), 1 resulting in the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2 ) to the two second messengers, inositol 1,4,5-trisphosphate (Ins(1,4,5)P 3 ) and diacylglycerol, which induce Ca 2ϩ release from internal stores and stimulate protein kinase C, respectively (1, 2). During the last decade, it has become evident that in addition to serving as precursors to Ins(1,4,5)P 3 and diacylglycerol, phosphoinositides actively participate in other cellular functions: they have been shown to regulate the dynamics of the actin cytoskeleton through the interaction with actin-binding proteins (3, 4), and to potentiate the activation of protein kinase C (5) and PI-PLC (6, 7). In addition, phosphoinositides phosphorylated at the D 3 -hydroxy group of the inositol headgroup are required for specific vesicle trafficking steps (8, 9) and are able to activate the recently identified novel protein kinases Akt/PKB and phosphoinositide-dependent kinases (10). Recently, a new 3-phosphorylated phosphoinositide, phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P 2 ), was identified and shown to accumulate in yeast cells ...

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A Plant 126-kDa Phosphatidylinositol 4-Kinase with a Novel Repeat Structure

Cited by 67 publications

References 59 publications

A wheat PI4K gene whose product possesses threonine autophophorylation activity confers tolerance to drought and salt in Arabidopsis

A wheat PI4K gene whose product possesses threonine autophophorylation activity confers tolerance to drought and salt in Arabidopsis

Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae

Salinity and Hyperosmotic Stress Induce Rapid Increases in Phosphatidylinositol 4,5-Bisphosphate, Diacylglycerol Pyrophosphate, and Phosphatidylcholine in Arabidopsis thaliana Cells

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