ZmcPKC70, a Protein Kinase C-type Enzyme from Maize

Chandok, Meena R.; Sopory, Sudhir K.

doi:10.1074/jbc.273.30.19235

Cited by 37 publications

(15 citation statements)

References 71 publications

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“…Although PKC-like enzyme activity has been shown in plants (Subramaniam et al, 1997), its corresponding gene in the Arabidopsis genome has not been identified. However, diacyl glyceroldependent PKC homologous genes have been isolated from other plants, and showed to function in plant defense responses including production of defensive secondary metabolites (Chandok and Sopory, 1998;Subramaniam et al, 1997;Vasconsuelo et al, 2003Vasconsuelo et al, , 2004. In this work, the complete inhibition of lead-induced ROS production by the calmodulin inhibitor W7 (Figure 7) suggested the role of calmodulin in NADPH-oxidase-like enzyme activation.…”

Section: Discussionmentioning

confidence: 78%

Potential role of NADPH-oxidase in early steps of lead-induced oxidative burst in Vicia faba roots

Pourrut

Perchet

Silvestre

et al. 2008

Journal of Plant Physiology

123

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Section: Discussionmentioning

confidence: 78%

Potential role of NADPH-oxidase in early steps of lead-induced oxidative burst in Vicia faba roots

Pourrut

Perchet

Silvestre

et al. 2008

Journal of Plant Physiology

123

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“…The kinase activity of this enzyme was stimulated by calcium, PtdSer and oleyl-acetyl-glycerol or PMA. Moreover, it was shown that the labelled [ 3 H]PMA is able to bind to purified protein kinase [16]. A protein kinase resembling the mammalian PKC has been also partly purified from Brassica campestris seedlings.…”

Section: Discussionmentioning

confidence: 99%

“…Our data do not exclude the possibility of the presence in plants of a structural homolog of PKC. Recently a protein kinase of apparent molecular mass of 70 kDa was purified from etiolated leaves of maize [16]. The kinase activity of this enzyme was stimulated by calcium, PtdSer and oleyl-acetyl-glycerol or PMA.…”

Section: Discussionmentioning

confidence: 99%

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Calcium‐dependent protein kinase from maize seedlings activated by phospholipids

Szczegielniak

Liwosz

Jurkowski

et al. 2000

European Journal of Biochemistry

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A calcium-and phospholipid-dependent protein kinase of apparent molecular mass 54 kDa (designated ZmCPKp54) was partially purified from etiolated maize seedlings. Activity of ZmCPKp54 is stimulated by phosphatidylserine and phosphatidylinositol, but is not essentially affected by diolein and phorbol esters. The enzyme cross-reacts with polyclonal antibodies against the calmodulin like-domain of the calcium-dependent protein kinase, but not with antibodies against catalytic or regulatory domains of protein kinase C. ZmCPKp54 is not able to phosphorylate the specific substrates of protein kinase C (MARCKS peptide and protein kinase C substrate peptide derived from pseudosubstrate sequence) and its activity is not inhibited by specific PKC inhibitors (bisindolylmaleimide, protein kinase C pseudosubstrate inhibitory peptide). The substrate specificity and sensitivity to the inhibitors of the maize enzyme resembles calcium-dependent protein kinase. The biochemical and immunological properties indicate that ZmCPKp54 belongs to the calcium-dependent protein kinase family.Keywords: plant protein kinase; protein kinase specificity; calcium, phosphatidylserine; phosphatidylinositol. In addition, the rapid turnover of phosphatidylinositol (PtdIns) metabolites has been demonstrated in a variety of plant signal responses (reviewed in [2]). The phosphatidylinositol pathway involves stimulation of a phospholipase C and release of two messengers: diacylglycerol and inositol(1,4,5)-trisphosphate. Diacylglycerol and inositol(1,4,5)trisphosphate are widespread in plant cells, and the levels of diacylglycerol and inositol(1,4,5)trisphosphate are changed during leaf movement [3], when the plants are exposed to the light [4] or during osmotic stress [5,6]. In the animal kingdom the activity of protein kinase C (PKC) is dependent on calcium and phospholipids. It is involved in sensing the cellular changes of diacylglycerol and calcium ion concentrations, transducing the signal from the cell membrane to the other signalling components, and finally to the cell nucleus (reviewed in [7]).The presence of elements required for inositol phospholipidbased signalling in plant cells has prompted investigators to look for a calcium-and phospholipid-dependent protein kinase resembling mammalian PKC. The presence of a Ca 12 -and lipid-dependent kinase activity in plants was first shown in cytosolic fraction of zucchini (courgettes) [8] Recently, a 70-kDa protein kinase possessing activity that is stimulated by diacylglycerol or phorbol esters in the presence of calcium was purified to homogenity from etiolated maize leaves [16]. Moreover, a functional homolog of mammalian PKC was identified in potato as a key element in the elicitorinduced defence [18]. The above biochemical and immunological data suggest the existence of PKC counterpart in plants.A large family of calcium-dependent protein kinases (CDPKs), also called calmodulin-like domain protein kinases, is present in plants. These enzymes control many physiological responses and are involved ...

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“…동물에서 DAG는 Ca 2+ 을 통하여 protein kinase C (PKC)의 활성을 촉진하여 신호 자극이 protein phosphorylation-dephosphorylation 반응으로 전환된다 [14]. 한편, 옥수수에서도 protein kinase C-type (ZmcPKC70) 이 확인되고, 이 효소는 phorbol 12-myristate 13-acetate (PMA)에 의해 조절되며, staurosporine (STA)에 의해 억제되 었다 [2]. Szczegielniak (Fig.…”

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Regulation of Phorbol 12-Myristate 13-Acetate in the Gravitropic Response and Ethylene Production in Primary Roots of Maize

Jeong¹,

Kim²,

Lee³

et al. 2012

Journal of Life Science

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Phorbol 12-myristate 13-acetate (PMA), a known tumor-promoting phorbol ester, activates the signal transduction enzyme protein kinase C (PKC) in animal cells. We investigated the effect of PMA on the regulation of gravitropism via ethylene production in primary roots of maize. PMA stimulated root growth and the gravitropic response in a concentration-dependent manner at 10 -6 M and 10 -4 M over 8 hrs. These effects were prevented by treatment with staurosporine (STA), a potent inhibitor of PKC. These results support the possibility that the gravitropic response might be regulated through protein kinases that are involved in the signal transduction system. Ethylene is known to play a role in the regulation of root growth and gravitropism. Ethylene production was increased by about 26% and 37% of the control rate in response to 10 -6 M and 10 -4 M PMA, respectively. PMA also stimulated the activity of ACC synthase (ACS), which converts the S-adenosyl-L-methionine (AdoMet) to 1-aminocyclopropane-1-carboxylic acid (ACC) in the ethylene production pathway. These effects on ethylene production were also prevented by STA treatment. These results suggest that the root gravitropic response in maize is regulated through protein kinases via ethylene production.

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ZmcPKC70, a Protein Kinase C-type Enzyme from Maize

Cited by 37 publications

References 71 publications

Potential role of NADPH-oxidase in early steps of lead-induced oxidative burst in Vicia faba roots

Potential role of NADPH-oxidase in early steps of lead-induced oxidative burst in Vicia faba roots

Calcium‐dependent protein kinase from maize seedlings activated by phospholipids

Regulation of Phorbol 12-Myristate 13-Acetate in the Gravitropic Response and Ethylene Production in Primary Roots of Maize

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