Partial purification and properties of a protein kinase C type enzyme from plants

Elliott, Daphne C.; Kokke, Yasmin S.

doi:10.1016/s0031-9422(00)84565-3

Cited by 37 publications

(8 citation statements)

References 20 publications

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“…In a protein gel blot assay performed with our protein extract, an antibody raised against a peptide from the catalytic domain of the animal PKC cross-reacted with a protein of ‫05ف‬ kD (data not shown). This observation is consistent with reports that indicate a 50-kD species as the catalytic fragment of PKC (Elliot and Kokke, 1987;Subramaniam et al, 1997), and work is currently under way to further characterize this protein. Studies with tomato pollen tubes have shown that two genes encoding receptor-like protein kinases are pollen specific (Muschietti et al, 1998), and a similar tissue specificity may exist for our protein.…”

Section: Is a Protein Kinase C-type Enzyme Present In Pollen Tubes?supporting

confidence: 91%

“…On the other hand, Van der Hoeven et al (1996) detected in oat root plasma membranes a protein kinase that is activated by Ca 2ϩ and cis-unsaturated fatty acids, phosphorylating a synthetic peptide with a motif that can be a target for both PKC and CDPK. Elliot and Kokke (1987) also purified a PKC-type enzyme with dependence on micromolar concentrations of free Ca 2ϩ from seedlings of Amaranthus tricolor. The properties of this enzyme include phospholipid activation and reaction with antibodies raised against the regulatory domain of bovine brain PKC.…”

Section: Is a Protein Kinase C-type Enzyme Present In Pollen Tubes?mentioning

confidence: 99%

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Relocation of a Ca²-Dependent Protein Kinase Activity during Pollen Tube Reorientation

1998

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Pollen tube reorientation is a dynamic cellular event that is crucial for successful fertilization. We have shown previously that pollen tube orientation is regulated by cytosolic free calcium ([Ca 2 ؉ ] c ). In this paper, we studied the activity of a Ca 2 ؉ -dependent protein kinase during reorientation. The kinase activity was assayed in living cells by using confocal ratio imaging of BODIPY FL bisindolylmaleimide. We found that growing pollen tubes exhibited higher protein kinase activity in the apical region, whereas nongrowing cells showed uniform distribution. Modification of growth direction by diffusion of inhibitors/activators from a micropipette showed the spatial redistribution of kinase activity to predict the new growth orientation. Localized increases in [Ca 2 ؉ ] c induced by photolysis of caged Ca 2 ؉ that led to reorientation also increased kinase activity. Molecular and immunological assays suggest that this kinase may show some functional homology with protein kinase C. We suggest that the tip-localized gradient of kinase activity promotes Ca 2 ؉ -mediated exocytosis and may act to regulate Ca 2 ؉ channel activity. INTRODUCTIONSuccessful fertilization in the angiosperms depends on pollen tubes finding their way to the ovule. Pollen tubes frequently change their direction of growth until they finally reach the micropyle. Previously (Malhó et al., 1994Malhó and Trewavas, 1996), we have shown that the distribution of cytosolic free calcium ([Ca 2 ϩ ] c ) in the apical region and Ca 2 ϩ influx by asymmetric activity of Ca 2 ϩ channels play crucial roles in this process. However, the downstream processes involved in signal transduction are not known (Feijó et al., 1995;Trewavas and Malhó, 1997).Phosphorylation cascades are known to be a major part of signaling pathways in plant cells, particularly those involving Ca 2 ϩ (Trewavas and Malhó, 1997). However, methods for imaging protein kinase in living cells are limited. Olds et al. (1995) used the fluorescent dye NBD-phorbol acetate to visualize the activation of protein kinase C (PKC) in living cells. This dye interacts directly with the protein, and the authors showed that when the cells were incubated in a solution of low-dye concentration, they remained viable and performed their physiological functions; continued protein synthesis and turnover might prevent the inactivation of significant amounts of the protein kinase by interaction with the dye. However, NBD-phorbol acetate is a single-wavelength dye, which makes quantitation difficult because it was designed primarily to label PKC. Despite the importance of this enzyme in the regulation of animal cell metabolism, direct sequence equivalents in plant cells have yet to be identified. Nevertheless, there is evidence for lipid-activated kinases that might represent functional equivalents (Nanmori et al., 1994; AboEl-Saad and Wu, 1995;Sokolova et al., 1997;Subramaniam et al., 1997). The loading of fluorescently labeled peptides (syntide-2) recently has been used to map the distribution of a membe...

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Section: Is a Protein Kinase C-type Enzyme Present In Pollen Tubes?supporting

confidence: 91%

Section: Is a Protein Kinase C-type Enzyme Present In Pollen Tubes?mentioning

confidence: 99%

Relocation of a Ca²-Dependent Protein Kinase Activity during Pollen Tube Reorientation

1998

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“…The (12). In the presence of 1 gM Ca2 , shown to be required for activity, 40 ,ug phosphatidylserine/mL and 8 ,ug diolein/mL greatly enhanced the ability of the kinase to phosphorylate histone.…”

Section: Dg and Dg Kinasementioning

confidence: 94%

Transmembrane Signaling via Phosphatidylinositol 4,5-Bisphosphate Hydrolysis in Plants

Einspahr¹,

Thompson²

1990

Plant Physiol.

101

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Recent investigations have confirmed the presence of the polyphosphoinositides, phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate (PIP2), as well as inositol phospholipid-specific phospholipase C in higher plant and microalgal cells. In addition, it has been shown that stimulation of some photosynthetic cell types by environmental or hormonal challenge is accompanied by degradation of the polyphosphoinositides. The products of phospholipase C-catalyzed PIP2 hydrolysis, inositol 1,4,5-trisphosphate and diacylglycerol, appear to (24). In the limited space available, this short review will (a) highlight selected new developments during the past 2 years, (b) identify possible sources of confusion and areas in need of clarification, and (c) preview potentially significant research areas of the future.The basic process of transmembrane signaling via the inositol phospholipids as it is understood in nonphotosynthetic cells is outlined in Figure 1. Recent evidence suggesting an involvement ofthis signaling pathway in plants is summarized below. EVIDENCE FOR COMPONENTS OF THE SIGNALING PATHWAY IN PLANTS Stimulation by Extracellular SignalsDespite the expected participation of a plasma membraneassociated receptor in plant PIP2-mediated signal transduction, no such receptor has been identified. In

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“…Similar calcium and phospholipid-dependent kinase activity has earlier been demonstrated in the cytosolic fractions of zucchini, oat, Amaranthus tricolor, and rice. [25][26][27][28] Specific isoforms of "conventional" PKC (α, β, and γ) are modulated by calcium. A probable crosstalk between ROS and PKC seems likely from earlier investigations on animal systems, with calcium ions regulating both PKC activity and ROS homeostasis through various scavenging mechanisms (Fig.…”

mentioning

confidence: 99%

A probable crosstalk between Ca⁺², reactive oxygen species accumulation and scavenging mechanisms and modulation of protein kinase C activity during seed development in sunflower

Thakur

Bhatla

2014

Plant Signaling & Behavior

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Partial purification and properties of a protein kinase C type enzyme from plants

Cited by 37 publications

References 20 publications

Relocation of a Ca²-Dependent Protein Kinase Activity during Pollen Tube Reorientation

Relocation of a Ca²-Dependent Protein Kinase Activity during Pollen Tube Reorientation

Transmembrane Signaling via Phosphatidylinositol 4,5-Bisphosphate Hydrolysis in Plants

A probable crosstalk between Ca⁺², reactive oxygen species accumulation and scavenging mechanisms and modulation of protein kinase C activity during seed development in sunflower

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Partial purification and properties of a protein kinase C type enzyme from plants

Cited by 37 publications

References 20 publications

Relocation of a Ca2-Dependent Protein Kinase Activity during Pollen Tube Reorientation

Relocation of a Ca2-Dependent Protein Kinase Activity during Pollen Tube Reorientation

Transmembrane Signaling via Phosphatidylinositol 4,5-Bisphosphate Hydrolysis in Plants

A probable crosstalk between Ca+2, reactive oxygen species accumulation and scavenging mechanisms and modulation of protein kinase C activity during seed development in sunflower

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Relocation of a Ca²-Dependent Protein Kinase Activity during Pollen Tube Reorientation

Relocation of a Ca²-Dependent Protein Kinase Activity during Pollen Tube Reorientation

A probable crosstalk between Ca⁺², reactive oxygen species accumulation and scavenging mechanisms and modulation of protein kinase C activity during seed development in sunflower