MsERK1: A Mitogen-Activated Protein Kinase from a Flowering Plant

Duerr, Barbara; Gawienowski, Margaret; Ropp, Traci; Jacobs, Thomas

doi:10.2307/3869431

Cited by 9 publications

(14 citation statements)

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“…For example, other plant protein kinases, such as tobacco protein kinases NPK5 and calcium-dependent protein kinase (CDPK), that apparently do not belong to the MAP kinase family are known to phosphorylate MBP and/or synthetic peptides derived from MBP (47,48). Although many cDNAs that encode putative members of the MAP kinase family have been isolated from various plants (5)(6)(7)(8)(9)(10), the characteristics of the active forms of the corresponding proteins have not yet been examined. Recently, novel kinases called SAPKs or JNKs, which have been grouped in a MAP kinase subfamily on the basis of their amino acid sequences, have been isolated from mammalian cells, but they failed to phosphorylate MBP (49,50).…”

Section: Discussionmentioning

confidence: 99%

“…Signal pathways known as mitogen-activated protein (MAP) kinase cascades have been established recently in yeasts and animals and shown to be involved in various physiological processes (1)(2)(3)(4). Furthermore, several groups including our own have shown that plants also have homologs of the components of the MAP kinase cascade (5)(6)(7)(8)(9)(10)(11)(12). Thus, it would seem likely that MAP kinase cascades occur in plants even though the relationships among these plant homologs have yet to be determined (13).…”

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confidence: 99%

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Cutting activates a 46-kilodalton protein kinase in plants.

Usami

Banno

Ito

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

169

118

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Using SDS/polyacrylamide gels that contained myelin basic protein, we identified a 46-kDa protein kinase in tobacco that is transiently activated by cutting. Although the activity of the kinase was rarely detectable in mature leaves, marked activity became apparent within several minutes after isolation of leaf discs and subsided within 30 min. In the presence of cycloheximide (CHX), the kinase activity did not diminish after the isolation over the course of 2 hr, suggesting that protein synthesis was not required for the activation of the kinase. A second cutting of leaf discs between 30 min and 60 min' after the isolation failed to activate the kinase, whereas a second cutting given 3 hr after isolation apparently activated the kinase. These results suggest that the 46-kDa protein kinase is desensitized immediately after the first activation, which can be blocked by CHX, but the response ability recovers with time. When protein extracts containing the active kinase were treated with serine/threonine-specific or tyrosine-specific protein phosphatase, the kinase activity was abolished. After immunoprecipitation with antibody against phosphotyrosine, activity of the kinase was recovered in the immunoprecipitate. These results suggest that the active form of the kinase is phosphorylated at both serine/threonine and tyrosine residues. It seems likely that the 46-kDa protein kinase can be activated by dual phosphorylation. The activity of a 46-kDa protein kinase was also detected in leaves of a wide variety of plant species including dicotyledonous and monocotyledonous plants. We propose the name PMSAP (plant multiaignal-activated protein) kinase for this kinase because the kinase was also activated by various signals other than cutting.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Cutting activates a 46-kilodalton protein kinase in plants.

Usami

Banno

Ito

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

169

118

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“…Many plant genes encode receptor kinases sharing the same basic domain structures as shown in animal receptors and are called RLKs. 1 Plant RLKs are involved in diverse processes such as hormone response (7), mitogenic induction (8), self-incompatibility (9), shoot meristem development (10), and disease resistance (11). Expression studies have implicated RLKs to be involved in embryogenesis, pollen function, and light responses (12).…”

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confidence: 99%

Role of Threonines in the Arabidopsis thaliana Somatic Embryogenesis Receptor Kinase 1 Activation Loop in Phosphorylation

Shah¹,

Vervoort²,

Vries³

2001

Journal of Biological Chemistry

106

124

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The Arabidopsis thaliana somatic embryogenesis receptor kinase 1 (AtSERK1) gene encodes a receptor-like protein kinase that is transiently expressed during embryogenesis. To determine the intrinsic biochemical properties of the AtSERK1 protein, we have expressed the intracellular catalytic domain as a glutathione S-transferase fusion protein in Escherichia coli. The AtSERK1-glutathione S-transferase fusion protein mainly autophosphorylates on threonine residues (K m for ATP, 4 ؋ 10 ؊6 M), and the reaction is Mg 2؉ dependent and inhibited by Mn 2؉ . A K330E substitution in the kinase domain of AtSERK1 abolishes all kinase activity. The active AtSERK1 kin can phosphorylate inactive AtSERK1 K330E protein, suggesting an intermolecular mechanism of autophosphorylation. The AtSERK1 kinase protein was modeled using the insulin receptor kinase as a template. On the basis of this model, threonine residues in the AtSERK1 activation loop of catalytic subdomain VIII are potential targets for phosphorylation. AtSERK1 phosphorylation on myelin basic protein and casein showed tyrosine, serine, and threonine as targets, demonstrating that AtSERK1 is a dual specificity kinase. Replacing Thr-468 with either alanine or glutamic acid not only obliterated the ability of the AtSERK1 protein to be phosphorylated but also inhibited phosphorylation on myelin basic protein and casein, suggesting that Thr-468 is essential for AtSERKmediated signaling.Perception and transduction of external stimuli are essential for the growth and development of multicellular organisms. In many cases this involves membrane-associated receptor proteins of which the ligand binding domains perceive the extracellular signal molecule. Information is then transmitted through the kinase domains of the receptor that in turn lead to phosphorylation of target proteins (1, 2). Most animal receptor kinases have tyrosine kinase activity, only a few are serine/ threonine kinases (2, 3) or can phosphorylate serine and threonine in addition to tyrosine (4). There is increasing evidence that protein kinases also play important roles in cellular signaling and metabolic regulation in plants. Rapid and transient changes in the phosphorylation pattern of plant membraneassociated proteins have indicated the involvement of protein kinases in signaling events (5, 6). Many plant genes encode receptor kinases sharing the same basic domain structures as shown in animal receptors and are called RLKs.

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“…However, it is unclear whether this antibody also recognizes alfalfa MMK1. MMK1 is a member of another distinct group of plant MAP kinase represented by SIPK from tobacco (20,28,29). MMK1 shares 8 of 10 C-terminal amino acids with MMK4.…”

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confidence: 99%

The tobacco wounding-activated mitogen-activated protein kinase is encoded by SIPK

Zhang

Klessig

1998

Proc. Natl. Acad. Sci. U.S.A.

222

167

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It has been demonstrated that both salicylic acid and fungal elicitors activate a 48-kDa mitogen-activated protein kinase termed salicylic acid-induced protein kinase (SIPK) in tobacco suspension cells. Here, we show that infiltration of these agents into tobacco leaves also activates SIPK. Of particular interest, infiltration of water alone activated a kinase of the same size, possibly because of wounding and͞or osmotic stresses. The kinetics of kinase activation, however, differ for these different treatments. Various mechanical stresses, including cutting and wounding by abrasion, also activated a 48-kDa kinase. By using an immunecomplex kinase assay with antibodies specific for SIPK or wounding-induced protein kinase, we demonstrate that this wounding-activated 48-kDa kinase is SIPK, rather than wounding-induced protein kinase, as reported [Seo, S., Okamoto, M.,

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MsERK1: A Mitogen-Activated Protein Kinase from a Flowering Plant

Cited by 9 publications

References 0 publications

Cutting activates a 46-kilodalton protein kinase in plants.

Cutting activates a 46-kilodalton protein kinase in plants.

Role of Threonines in the Arabidopsis thaliana Somatic Embryogenesis Receptor Kinase 1 Activation Loop in Phosphorylation

The tobacco wounding-activated mitogen-activated protein kinase is encoded by SIPK

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