Protein Kinases in Zucchini (Characterization of Calcium-Requiring Plasma Membrane Kinases)

Verhey, SD; Gaiser, J. Christopher; Lomax, Terri L.

doi:10.1104/pp.103.2.413

Cited by 35 publications

(27 citation statements)

References 29 publications

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“…In recent years, many articles have reported the presence of a wide range of protein kinases in plant tissues, both soluble (Polya and Micucci, 1985;Lu et al, 1996) and associated with the plasma membrane (Verhey et al, 1993). Schaller and co-workers (1992) reported that unlike animal cells, the predominant Ca 2ϩ and lipid-dependent protein kinase associated with the plasma membrane of oat cells has biochemical properties and amino acid sequence unlike PKC.…”

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

confidence: 99%

“…Currently, the most thoroughly investigated plant kinases are CDPKs. Some are found attached to the plasma membrane (Verhey et al, 1993) and some to the cytoskeleton (Putnam-Evans et al, 1989), and some are soluble (Polya and Micucci, 1985). A protein of this family has been found in pollen tubes (Estruch et al, 1994), thus suggesting its involvement in tip growth.…”

Section: Introductionmentioning

confidence: 99%

“…In animal cells, PKC is a vital element in these pathways. It is a known regulator of Ca 2 ϩ -dependent exocytosis (Burgoyne and Morgan, 1993), and it was shown to regulate Ca 2ϩ influx by modification of channel activity (Petersen and Berridge, 1994).In recent years, many articles have reported the presence of a wide range of protein kinases in plant tissues, both soluble (Polya and Micucci, 1985;Lu et al, 1996) and associated with the plasma membrane (Verhey et al, 1993). Schaller and co-workers (1992) reported that unlike animal cells, the predominant Ca 2ϩ and lipid-dependent protein kinase associated with the plasma membrane of oat cells has biochemical properties and amino acid sequence unlike PKC.…”

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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?mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

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

1998

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“…CDPKs exist as multiple isoforms 17) and isolation of cDNA further revealed that these enzymes are encoded by a multigene family. 18,19) As for their localization, CDPKs are either membrane-associated 20,21) or cytosolic in nature.…”

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confidence: 99%

“…As a specific group of kinases CDPKs require only micromolar concentrations of Ca 2ϩ for their activity, do not require calmodulin or phospholipids in plants and have been identified as Ca 2ϩ -dependent and calmodulin-independent serine/threonine kinases. 14,15) The plant CDPKs have been shown to phosphorylate a number of exogenous substrates, including histone III-S. 16) CDPKs exist as multiple isoforms 17) and isolation of cDNA further revealed that these enzymes are encoded by a multigene family. 18,19) As for their localization, CDPKs are either membrane-associated 20,21) or cytosolic in nature.…”

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Characterization of a Ca2+-Dependent Protein Kinase from Rice Root: Differential Response to Cold and Regulation by Abscisic Acid.

Komatsu

Konishi

et al. 2001

Biological & Pharmaceutical Bulletin

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Plants can respond to a variety of biotic and abiotic signals or factors that affect their growth and development. Although the responses to these signals and factors in plants have been extensively studied at physiological and biochemical levels, the perception and intracellular transmission mechanisms remain largely unknown. Under natural growth conditions, plants do encounter various stress conditions such as drought, salinity, and high or low temperature, which have profound effects on their growth and development. Rice seedlings can respond to cold treatment with major changes in gene expression.1) It is generally recognized that patterns of protein synthesis and mRNA level change when plants are exposed to cold.2) Various stress conditions have been shown to influence protein phosphorylation. 3,4) During the early stages of cold acclimation, phosphorylation of cellular proteins and activation of protein kinases have been detected. 5)In our earlier study, the 60 kDa protein was independently phosphorylated in cold-tolerant Japonica varieties in cold treatment, but this phosphorylation is induced in cold-sensitive Indica varieties. 6) Recently, it has been reported that rice seedlings respond to cold stress of 5°C by definite changes in protein phosphorylation. 7) This suggests that subjecting rice seedlings to low temperatures results in a variety of biochemical changes at the cellular level.Low temperature treatment has been shown to induce an increase in cytosolic Ca 2ϩ levels, 8,9) and Ca 2ϩ could play an essential role in the cold-acclimation process.10,11) Ca 2ϩ plays important roles in numerous physiological processes and the presence of Ca 2ϩ -regulated protein kinases will have wider implications in cellular signal transduction.12,13) Ca 2ϩ -dependent protein kinases (CDPKs) play a key role in stress and Ca 2ϩ -mediated signal transduction. As a specific group of kinases CDPKs require only micromolar concentrations of Ca 2ϩ for their activity, do not require calmodulin or phospholipids in plants and have been identified as Ca 2ϩ -dependent and calmodulin-independent serine/threonine kinases.14,15)The plant CDPKs have been shown to phosphorylate a number of exogenous substrates, including histone III-S. 16)CDPKs exist as multiple isoforms 17) and isolation of cDNA further revealed that these enzymes are encoded by a multigene family. 18,19) As for their localization, CDPKs are either membrane-associated 20,21) or cytosolic in nature. 22,23) A 32 kDa CDPK was detected during regeneration of rice cultured suspension cells by an in-gel kinase assay.24) Also a 45 kDa Ca 2ϩ -and phospholipid-dependent protein kinases in rice embryos and leaves were identified in previous studies.25) A 45 kDa CDPK, which can phosphorylate histone III-S in gel, was found in rice leaf under darkness in the presence of Ca 2ϩ and phosphatidylserine 26) ; their functions, however, remain to be clarified. Rice seedlings under cold stress induce a 47 kDa CDPK in an increasing manner in leaf sheath tissues. 27) However, the functi...

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Biologically Active Lipids and Lipid-modulated Protein Kinase in Plants

Scherer¹

1996

Signal Transduction in Plant Growth and Development

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Protein Kinases in Zucchini (Characterization of Calcium-Requiring Plasma Membrane Kinases)

Cited by 35 publications

References 29 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

Characterization of a Ca2+-Dependent Protein Kinase from Rice Root: Differential Response to Cold and Regulation by Abscisic Acid.

Biologically Active Lipids and Lipid-modulated Protein Kinase in Plants

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Protein Kinases in Zucchini (Characterization of Calcium-Requiring Plasma Membrane Kinases)

Cited by 35 publications

References 29 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

Characterization of a Ca2+-Dependent Protein Kinase from Rice Root: Differential Response to Cold and Regulation by Abscisic Acid.

Biologically Active Lipids and Lipid-modulated Protein Kinase in Plants

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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