Mitogen-activated protein (MAP) kinase signalling in plant environmental stress responses

2011 ◽  
Vol 59 (3) ◽  
pp. 285-290
Author(s):  
R. Dóczi
Keyword(s):  
Environmental Stress ◽  
Map Kinase ◽  
Stress Responses ◽  
Map Kinases ◽  
Wide Range ◽  
Protein Map ◽  
Genes Encoding ◽  
Mitogen Activated Protein ◽  
Extracellular Stimuli ◽  
Stress Signalling

Due to their sessile life style plants have to cope with a variety of unfavourable environmental conditions. Extracellular stimuli are perceived by specific sensors and receptors and are transmitted within the cell by various signal transduction pathways to trigger appropriate responses. The mitogen-activated protein (MAP) kinase cascades are well-conserved signalling pathway modules found in all eukaryotes. Activated MAP kinases phosphorylate an array of substrate proteins. Phosphorylation results in altered substrate activities that mediate a wide range of responses, including changes in gene expression. The genome of the model plant Arabidopsis thaliana contains genes encoding 20 mitogen-activated protein kinases and 10 MAPK kinases. In plants MAP kinases play a central role in environmental stress signalling; however, our knowledge mainly comes from results on three MAP kinases and their immediate upstream activators. Further studies on additional members of the plant MAP kinase repertoire together with the identification of downstream substrates and connections to specific upstream signal receptors are required to elucidate their specific functions within environmental stress signalling networks. Understanding the mechanisms of specificity in signal flow is indispensable for engineering improved crops with modified MAP kinase signalling for agricultural purposes.

scholarly journals c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases.

1994 ◽  
Vol 14 (10) ◽  
pp. 6683-6688 ◽  
Author(s):  
A Minden ◽  
A Lin ◽  
T Smeal ◽  
B Dérijard ◽  
M Cobb ◽  
...  
Keyword(s):  
Map Kinase ◽  
Map Kinases ◽  
New Members ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Extracellular Stimuli ◽  
Terminal Site ◽  
Stimulation Of

c-Jun transcriptional activity is stimulated by phosphorylation at two N-terminal sites: Ser-63 and -73. Phosphorylation of these sites is enhanced in response to a variety of extracellular stimuli, including growth factors, cytokines, and UV irradiation. New members of the mitogen-activated protein (MAP) kinase group of signal-transducing enzymes, termed JNKs, bind to the activation domain of c-Jun and specifically phosphorylate these sites. However, the N-terminal sites of c-Jun were also suggested to be phosphorylated by two other MAP kinases, ERK1 and ERK2. Despite these reports, we find that unlike the JNKs, ERK1 and ERK2 do not phosphorylate the N-terminal sites of c-Jun in vitro; instead they phosphorylate an inhibitory C-terminal site. Furthermore, the phosphorylation of c-Jun in vivo at the N-terminal sites correlates with activation of the JNKs but not the ERKs. The ERKs are probably involved in the induction of c-fos expression and thereby contribute to the stimulation of AP-1 activity. Our study suggests that two different branches of the MAP kinase group are involved in the stimulation of AP-1 activity through two different mechanisms.

c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases

1994 ◽  
Vol 14 (10) ◽  
pp. 6683-6688
Author(s):  
A Minden ◽  
A Lin ◽  
T Smeal ◽  
B Dérijard ◽  
M Cobb ◽  
...  
Keyword(s):  
Map Kinase ◽  
Map Kinases ◽  
New Members ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Extracellular Stimuli ◽  
Terminal Site ◽  
Stimulation Of

c-Jun transcriptional activity is stimulated by phosphorylation at two N-terminal sites: Ser-63 and -73. Phosphorylation of these sites is enhanced in response to a variety of extracellular stimuli, including growth factors, cytokines, and UV irradiation. New members of the mitogen-activated protein (MAP) kinase group of signal-transducing enzymes, termed JNKs, bind to the activation domain of c-Jun and specifically phosphorylate these sites. However, the N-terminal sites of c-Jun were also suggested to be phosphorylated by two other MAP kinases, ERK1 and ERK2. Despite these reports, we find that unlike the JNKs, ERK1 and ERK2 do not phosphorylate the N-terminal sites of c-Jun in vitro; instead they phosphorylate an inhibitory C-terminal site. Furthermore, the phosphorylation of c-Jun in vivo at the N-terminal sites correlates with activation of the JNKs but not the ERKs. The ERKs are probably involved in the induction of c-fos expression and thereby contribute to the stimulation of AP-1 activity. Our study suggests that two different branches of the MAP kinase group are involved in the stimulation of AP-1 activity through two different mechanisms.

scholarly journals Selective activation of p42 mitogen-activated protein (MAP) kinase in murine B lymphoma cell lines by membrane immunoglobulin cross-linking. Evidence for protein kinase C-independent and -dependent mechanisms of activation

1992 ◽  
Vol 287 (1) ◽  
pp. 269-276 ◽  
Author(s):  
M R Gold ◽  
J S Sanghera ◽  
J Stewart ◽  
S L Pelech
Keyword(s):  
Map Kinase ◽  
Tyrosine Phosphorylation ◽  
Cell Lines ◽  
Map Kinases ◽  
Phorbol Esters ◽  
Cross Linking ◽  
Kinase Activation ◽  
Membrane Immunoglobulin ◽  
Protein Map ◽  
Mitogen Activated Protein

Cross-linking of membrane immunoglobulin (mIg), the B lymphocyte antigen receptor, with anti-receptor antibodies stimulates tyrosine phosphorylation of a number of proteins, including one of 42 kDa. Proteins with a similar molecular mass are tyrosine-phosphorylated in response to receptor stimulation in other cell types and have been identified as serine/threonine kinases, termed mitogen-activated protein (MAP) kinases or extracellular signal-regulated kinases (ERKs). The MAP kinases constitute a family of related kinases, at least three of which have molecular masses of 40-45 kDa. In this paper we show that mIg cross-linking stimulated the myelin basic protein phosphotransferase activity characteristic of MAP kinase in both mature and immature murine B cell lines. This enzyme activity co-purified on three different columns with a 42 kDa protein that was tyrosine-phosphorylated (pp42) in response to mIg cross-linking and which reacted with a panel of anti-(MAP kinase) antibodies. Although immunoblotting with the anti-(MAP kinase) antibodies showed that these B cell lines expressed both 42 kDa and 44 kDa forms of MAP kinase, only the 42 kDa form was activated and tyrosine-phosphorylated to a significant extent. Activation of protein kinase C (PKC) with phorbol esters also resulted in selective tyrosine phosphorylation and activation of the 42 kDa MAP kinase. This suggested that mIg-induced MAP kinase activation could be due to stimulation of PKC by mIg. However, mIg-stimulated MAP kinase activation and pp42 tyrosine phosphorylation was only partially blocked by a PKC inhibitor, the staurosporine analogue Compound 3. In contrast, Compound 3 completely blocked the ability of phorbol esters to stimulate MAP kinase activity and induce tyrosine phosphorylation of pp42. Thus mIg may activate MAP kinase by both PKC-dependent and -independent mechanisms.

scholarly journals BWMK1, a Novel MAP Kinase Induced by Fungal Infection and Mechanical Wounding in Rice

1999 ◽  
Vol 12 (12) ◽  
pp. 1064-1073 ◽  
Author(s):  
Chaozu He ◽  
Steven Haw Tien Fong ◽  
Daichang Yang ◽  
Guo-Liang Wang
Keyword(s):  
Map Kinase ◽  
Map Kinases ◽  
Magnaporthe Grisea ◽  
Mechanical Wounding ◽  
C Terminus ◽  
Acid Protein ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Rice Leaves ◽  
Activation Motif

The activation of the mitogen-activated protein (MAP) kinases by different environmental stresses has been previously observed in several dicot plant species. Here, we report the isolation of a novel MAP kinase in rice that is induced during infection by the blast fungus Magnaporthe grisea or upon mechanical wounding. The gene is designated as BWMK1 for blast- and wound-induced MAP kinase. The cDNA of BWMK1 was isolated from rice leaves challenged by the blast pathogen. Transcripts of the corresponding gene accumulated in rice leaves 4 h after blast inoculation and 30 min after mechanical wounding. This gene encodes a 506 amino acid protein that contains a new dual-phosphorylation activation motif TDY and about 150 unique amino acids on its C terminus. In-gel kinase activity and immunoprecipitation assays confirmed that BWMK1 is a functional MAP kinase. These results show that BWMK1 is a new member of the plant MAP kinase family and may mediate both defense and wound signaling in rice.

cAMP inhibits mitogen-activated protein (MAP) kinase activation and resumption of meiosis, but exerts no effects after spontaneous germinal vesicle breakdown (GVBD) in mouse oocytes

1999 ◽  
Vol 11 (2) ◽  
pp. 81 ◽  
Author(s):  
Q. Y. Sun ◽  
Q. Lu ◽  
H. Breitbart ◽  
D. Y. Chen
Keyword(s):  
Map Kinase ◽  
Map Kinases ◽  
Specific Inhibitor ◽  
Germinal Vesicle ◽  
Germinal Vesicle Breakdown ◽  
Kinase Activation ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Phosphorylation ◽  
Pkc Activation

Various signaling molecules have been implicated in the oocyte G2/MII transition, including protein kinase C (PKC), cAMP and mitogen-activated protein (MAP) kinases. However, the cross-talk among these signaling pathways has not been elucidated. The present study demonstrates that both germinal vesicle break down (GVBD) and MAP kinase phosphorylation (activation) are inhibited when intraoocyte cAMP is increased by treating the GV-intact oocytes with dibutyryl cyclic AMP (dbcAMP), forskolin, or isobutylmethylxanthine (IBMX). Okadaic acid, a specific inhibitor of protein phosphatase-1 and -2A, completely overcame this effect. Calphostin C, a specific inhibitor of PKC, accelerated both GVBD and MAP kinase phosphorylation, and this effect was attenuated by increased intraoocyte cAMP, whereas PKC activation inhibited these events. Once GVBD occurred, the progression of oocyte maturation and MAP kinase phosphorylation were independent of cAMP. These results indicate that an increase in intraoocyte cAMP, in synergy with PKC activation, initiates a cascade of events resulting in inhibition of MAP kinase phosphorylation and GVBD in the mouse oocyte.

Inhibition of p42 and p44 MAP kinase does not alter smooth muscle contraction in swine carotid artery

1998 ◽  
Vol 275 (1) ◽  
pp. H131-H138 ◽  
Author(s):  
Isabelle Gorenne ◽  
Xiaoling Su ◽  
Robert S. Moreland
Keyword(s):  
Smooth Muscle ◽  
Muscle Contraction ◽  
Map Kinase ◽  
Map Kinases ◽  
Kinase Activity ◽  
Smooth Muscle Contraction ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Phosphorylation

Caldesmon inhibits myosin ATPase activity; phosphorylation of caldesmon reverses the inhibition. The caldesmon kinase is believed to be mitogen-activated protein (MAP) kinase. MAP kinases are activated during vascular stimulation, but a cause-and-effect relationship between kinase activity and contraction has not been established. We examined the role of MAP kinase in contraction using PD-098059, an inhibitor of MAP kinase kinase (MEK). MAP kinase activity was assessed using an anti-active MAP kinase antibody and direct measurement of MAP kinase catalyzed phosphorylation of myelin basic protein, MBP-(95—98). MAP kinase phosphorylation, stimulated by histamine (50 μM) or phorbol 12,13-dibutyrate (PDBu, 0.1 μM), was inhibited by PD-098059 (100 μM). PD-098059 did not alter the sensitivity or the maximal level of force in smooth muscle stimulated by histamine or PDBu, nor did PD-098059 affect contraction of β-escin-permeabilized tissue. Our data suggest that p44 and p42 MAP kinases are not involved in regulation of vascular smooth muscle contraction. These results do not, however, preclude a role for other isoforms of the MAP kinase family.

scholarly journals Oxidation-triggered c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein (MAP) kinase pathways for apoptosis in human leukaemic cells stimulated by epigallocatechin-3-gallate (EGCG): a distinct pathway from those of chemically induced and receptor-mediated apoptosis

2002 ◽  
Vol 368 (3) ◽  
pp. 705-720 ◽  
Author(s):  
Koichi SAEKI ◽  
Norihiko KOBAYASHI ◽  
Yuko INAZAWA ◽  
Hong ZHANG ◽  
Hideki NISHITOH ◽  
...  
Keyword(s):  
Cell Death ◽  
Map Kinase ◽  
Map Kinases ◽  
Specific Inhibitor ◽  
P38 Map Kinase ◽  
Dominant Negative ◽  
Chemically Induced ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Induced Apoptosis

We investigated intracellular signalling pathways for apoptosis induced by epigallocatechin-3-gallate (EGCG) as compared with those induced by a toxic chemical substance (etoposide, VP16) or the death receptor ligand [tumour necrosis factor (TNF)]. EGCG as well as VP16 and TNF induced activation of two apoptosis-regulating mitogen-activated protein (MAP) kinases, namely c-Jun N-terminal kinase (JNK) and p38 MAP kinase, in both human leukaemic U937 and OCI-AML1a cells. In U937 cells, the apoptosis and activation of caspases-3 and −9 induced by EGCG but not VP16 and TNF were inhibited with SB203580, a specific inhibitor of p38, while those induced by EGCG and VP16 but not TNF were inhibited with SB202190, a rather broad inhibitor of JNK and p38. In contrast, the EGCG-induced apoptosis in OCI-AML1a cells was resistant to SB203580 but not to SB202190. Unlike TNF, EGCG did not induce the activation of nuclear factor-κB but rather induced the primary activation of caspase-9. N-Acetyl-l-cysteine (NAC) almost completely abolished apoptosis induced by EGCG under conditions in which the apoptosis induced by VP16 or TNF was not affected. The JNK/p38 activation by EGCG was also potently inhibited by NAC, whereas those by VP16 and TNF were either not or only minimally affected by NAC. In addition, dithiothreitol also suppressed both apoptosis and JNK/p38 activation by EGCG, and EGCG-induced activation of MAP kinase kinase (MKK) 3/6, MKK4 and apoptosis-regulating kinase 1 (ASK1) was suppressed by NAC. Dominant negative ASK1, MKK6, MKK4 and JNK1 potently inhibited EGCG-induced cell death. EGCG induced an intracellular increase in reactive oxygen species and GSSG, both of which were also inhibited by NAC, and the decreased synthesis of glutathione rendered the cell susceptible to EGCG-induced apoptosis. Taken together these results strongly suggest that EGCG executed apoptotic cell death via an ASK1, MKK and JNK/p38 cascade which is triggered by NAC-sensitive intracellular oxidative events in a manner distinct from chemically induced or receptor-mediated apoptosis.

scholarly journals The Colletotrichum lagenarium Ste12-Like Gene CST1 Is Essential for Appressorium Penetration

2003 ◽  
Vol 16 (4) ◽  
pp. 315-325 ◽  
Author(s):  
Gento Tsuji ◽  
Satoshi Fujii ◽  
Seiji Tsuge ◽  
Tomonori Shiraishi ◽  
Yasuyuki Kubo
Keyword(s):  
Map Kinase ◽  
Lipid Droplets ◽  
Map Kinases ◽  
Cellulose Membrane ◽  
Appressorium Formation ◽  
Colletotrichum Lagenarium ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Kinase Pathway

Colletotrichum lagenarium is the causal agent of anthracnose of cucumber. This fungus produces a darkly melanized infection structure, appressoria, to penetrate the host leaves. The C. lagenarium CMK1 gene, a homologue of the Saccharomyces cerevisiae FUS3/KSS1 mitogen-activated protein (MAP) kinase genes, was shown to regulate conidial germination, appressorium formation, and invasive growth. In S. cerevisiae, Ste12p is known to be a transcriptional factor downstream of Fus3p/Kss1p MAP kinases. To evaluate the CMK1 MAP kinase pathway, we isolated the Ste12 homologue CST1 gene from C. lagenarium and characterized. The cst1Δ strains were nonpathogenic on intact host leaves, but could form lesions when inoculated on wounded leaves. Conidia of the cst1Δ strains could germinate and form melanized appressoria on both host leaf surface and artificial cellulose membrane, but could not produce infectious hyphae from appressoria, suggesting that CST1 is essential for appressorium penetration in C. lagenarium. In addition, matured appressoria of the cst1Δ strains contained an extremely low level of lipid droplets compared with that of the wild-type strain. Lipid droplets were abundant in conidia of the cst1Δ strains, but rapidly disappeared during appressorium formation. This misscheduled lipid degradation might be related to the failure of appressorium penetration in the cst1Δ strain.

scholarly journals MAP Kinase Phosphatase-1 Protects against Inflammatory Bone Loss

2009 ◽  
Vol 88 (12) ◽  
pp. 1125-1130 ◽  
Author(s):  
R. Sartori ◽  
F. Li ◽  
K.L. Kirkwood
Keyword(s):  
Bone Loss ◽  
Map Kinase ◽  
Map Kinases ◽  
Group Analysis ◽  
P38 Map Kinase ◽  
Wild Type ◽  
Map Kinase Phosphatase ◽  
Tnf Α ◽  
Protein Map ◽  
Mitogen Activated Protein

The mitogen-activated protein (MAP) kinase phosphatase (MKP) family plays an important function in regulating the pro-inflammatory cytokines by deactivating MAP kinases. MKP-1 is essential for the dephosphorylation of p38 MAP kinase that regulates expression of IL-6, TNF-α, and IL-1β. We hypothesized that MKP-1 regulates inflammatory bone loss in experimental periodontitis. Wild-type and Mkp-1−/− mice received A. actinomycetemcomitans LPS injection in the palatal region or PBS control 3 times/wk for 30 days. Mice were killed, and maxillae were assessed by microcomputed tomography, histological analysis, and TRAP staining for measurement of bone loss, extent of inflammation, and degree of osteoclastogenesis. Results indicated that, in LPS-injected Mkp-1−/− mice, significantly greater bone loss occurred with more inflammatory infiltrate and a significant increase in osteoclastogenesis compared with Mkp-1−/− control sites or either wild-type group. Analysis of these data indicates that MKP-1 plays a key role in the regulation of inflammatory bone loss.

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