Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells
Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and act...
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| Autor*in: |
Wilson, Cathal [verfasserIn] Pfosser, Martin [verfasserIn] Jonak, Claudia [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Copenhagen: Munksgaard International Publishers ; 1998 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Physiologia plantarum - Oxford [u.a.] : Wiley-Blackwell, 1948, 102(1998), 4, Seite 0 |
| Übergeordnetes Werk: |
volume:102 ; year:1998 ; number:4 ; pages:0 |
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| DOI / URN: |
10.1034/j.1399-3054.1998.1020407.x |
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| 520 | |a Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. | ||
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| 700 | 1 | |a Vicente, Oscar |4 oth | |
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10.1034/j.1399-3054.1998.1020407.x doi (DE-627)NLEJ24379083X DE-627 ger DE-627 rakwb Wilson, Cathal verfasserin aut Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells Copenhagen Munksgaard International Publishers 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Cell cycle Pfosser, Martin verfasserin aut Jonak, Claudia verfasserin aut Hirt, Heribert oth Heberle-Bors, Erwin oth Vicente, Oscar oth In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 102(1998), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:102 year:1998 number:4 pages:0 http://dx.doi.org/10.1034/j.1399-3054.1998.1020407.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 102 1998 4 0 |
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10.1034/j.1399-3054.1998.1020407.x doi (DE-627)NLEJ24379083X DE-627 ger DE-627 rakwb Wilson, Cathal verfasserin aut Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells Copenhagen Munksgaard International Publishers 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Cell cycle Pfosser, Martin verfasserin aut Jonak, Claudia verfasserin aut Hirt, Heribert oth Heberle-Bors, Erwin oth Vicente, Oscar oth In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 102(1998), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:102 year:1998 number:4 pages:0 http://dx.doi.org/10.1034/j.1399-3054.1998.1020407.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 102 1998 4 0 |
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10.1034/j.1399-3054.1998.1020407.x doi (DE-627)NLEJ24379083X DE-627 ger DE-627 rakwb Wilson, Cathal verfasserin aut Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells Copenhagen Munksgaard International Publishers 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Cell cycle Pfosser, Martin verfasserin aut Jonak, Claudia verfasserin aut Hirt, Heribert oth Heberle-Bors, Erwin oth Vicente, Oscar oth In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 102(1998), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:102 year:1998 number:4 pages:0 http://dx.doi.org/10.1034/j.1399-3054.1998.1020407.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 102 1998 4 0 |
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10.1034/j.1399-3054.1998.1020407.x doi (DE-627)NLEJ24379083X DE-627 ger DE-627 rakwb Wilson, Cathal verfasserin aut Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells Copenhagen Munksgaard International Publishers 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Cell cycle Pfosser, Martin verfasserin aut Jonak, Claudia verfasserin aut Hirt, Heribert oth Heberle-Bors, Erwin oth Vicente, Oscar oth In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 102(1998), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:102 year:1998 number:4 pages:0 http://dx.doi.org/10.1034/j.1399-3054.1998.1020407.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 102 1998 4 0 |
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10.1034/j.1399-3054.1998.1020407.x doi (DE-627)NLEJ24379083X DE-627 ger DE-627 rakwb Wilson, Cathal verfasserin aut Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells Copenhagen Munksgaard International Publishers 1998 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Cell cycle Pfosser, Martin verfasserin aut Jonak, Claudia verfasserin aut Hirt, Heribert oth Heberle-Bors, Erwin oth Vicente, Oscar oth In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 102(1998), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:102 year:1998 number:4 pages:0 http://dx.doi.org/10.1034/j.1399-3054.1998.1020407.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 102 1998 4 0 |
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evidence for the activation of a map kinase upon phosphate-induced cell cycle re-entry in tobacco cells |
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Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells |
| abstract |
Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. |
| abstractGer |
Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. |
| abstract_unstemmed |
Mitogen-activated-protein (MAP) kinases are components of signal transduction pathways which respond to a variety of stimuli in different organisms. In quiescent mammalian cells, the reactivation of cell division induced by different mitogenic signals is mediated by the rapid phosphorylation and activation of MAP kinases. We have investigated whether a similar situation occurs in plants, arresting tobacco (Nicotiana tabacum L.) cells in the G1 phase of the cell cycle by phosphate starvation, and then inducing them to re-enter the cell cycle by refeeding with phosphate. The transient activation of a kinase activity with the characteristics of a MAP kinase was observed during the first hour after refeeding, when the cells were still in G1. Using myelin basic protein (MBP) as substrate, an increase in this phosphorylating activity, with a molecular mass of approximately 45 kDa, was detected in cell extracts between 35 and 55 min after induction, in in-gel phosphorylation assays and after immunoprecipitation with anti-MAP kinase antibodies. The specificity of the antibodies against recombinant tobacco MAP kinases suggested that the MAP kinase p45ntf4 was responsible for the observed activity. These data provide experimental evidence for the activation in vivo of a plant MAP kinase, possibly mediating the reactivation of cell division in G1-arrested cells. |
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Evidence for the activation of a MAP kinase upon phosphate-induced cell cycle re-entry in tobacco cells |
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Pfosser, Martin Jonak, Claudia Hirt, Heribert Heberle-Bors, Erwin Vicente, Oscar |
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