Identification, Characterization, and Expression Analysis Reveal Diverse Regulated Roles of Three MAPK Genes in Chlamys farreri Under Heat Stress

Mitogen-activated protein kinase (MAPK) cascades are fundamental signal transduction modules in all eukaryotic organisms, participating growth and development, as well as stress response. In the present study, three MAPK genes were successfully identified from the genome of Chlamys farreri, respectively, named CfERK1/2, CfJNK, and Cfp38, and only one copy of ERK, JNK, and p38 were detected. Domain analysis indicated that CfMAPKs possessed the typical domains, including S_TKc, Pkinase, and PKc_like domain. Phylogenetic analysis showed that three CfMAPKs of MAPK subfamilies exists in the common ancestor of vertebrates and invertebrates. All CfMAPKs specifically expressed during larval development and in adult tissues, and the expression level of CfERK1/2 and Cfp38 was apparently higher than that of CfJNK. Under heat stress, the expression of CfERK1/2 and Cfp38 were significantly downregulated and then upregulated in four tissues, while the expression of CfJNK increased in all tissues; these different expression patterns suggested a different molecular mechanism of CfMAPKs for bivalves to adapt to temperature changes. The diversity of CfMAPKs and their specific expression patterns provide valuable information for better understanding of the functions of MAPK cascades in bivalves.

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Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity

Biochemical Journal ◽

10.1042/bj20021806 ◽

2003 ◽

Vol 370 (3) ◽

pp. 1077-1085 ◽

Cited By ~ 67

Author(s):

A. Jane BARDWELL ◽

Mahsa ABDOLLAHI ◽

Lee BARDWELL

Keyword(s):

Transcription Factor ◽

Protein Kinase ◽

Protein Interactions ◽

Expression Patterns ◽

Enzymic Activity ◽

Mitogen Activated Protein Kinase ◽

Docking Site ◽

Mapk Cascades ◽

Mitogen Activated Protein ◽

Docking Sites

Mitogen-activated protein kinase (MAPK) cascades control gene expression patterns in response to extracellular stimuli. MAPK/ERK (extracellular-signal-regulated kinase) kinases (MEKs) activate MAPKs by phosphorylating them; activated MAPKs, in turn, phosphorylate target transcription factors, and are deactivated by phosphatases. One mechanism for maintaining signal specificity and efficiency is the interaction of MAPKs with their substrates and regulators through high-affinity docking sites. In the present study, we show that peptides corresponding to the MAPK-docking sites of MEK1, MEK2, Ste7, Elk-1 and MAPK phosphatase (MKP)-2 potently inhibit MEK2 phosphorylation of ERK2, ERK2 phosphorylation of Elk-1, and MKP-1 dephosphorylation of ERK2. Each peptide inhibited multiple reactions; for example, the MEK2 peptide inhibited not only MEK2, but also ERK2 and MKP-1. In addition, these docking-site peptides inhibited MEK2—ERK2 binding. The MAPK-docking site of MEK1 also potently stimulated ERK2-mediated phosphorylation of a target site on the same peptide. Control peptides with mutations of conserved basic and hydrophobic residues of the MAPK-docking site consensus lacked biological activity. We conclude that MEKs, MKPs and the Elk-1 transcription factor compete for binding to the same region of ERK2 via protein—protein interactions that are crucial for kinase/phosphatase activity.

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Chlorosis seedling lethality 1 encoding a MAP3K protein is essential for chloroplast development in rice

BMC Plant Biology ◽

10.1186/s12870-021-03404-9 ◽

2022 ◽

Vol 22 (1) ◽

Author(s):

Jiayan Liang ◽

Qiuxin Zhang ◽

Yiran Liu ◽

Jingjing Zhang ◽

Wenyi Wang ◽

...

Keyword(s):

Stress Responses ◽

Chloroplast Development ◽

Direct Interaction ◽

Mitogen Activated Protein Kinase ◽

Starch Granules ◽

Altered Expression ◽

Mapk Cascades ◽

Mitogen Activated Protein ◽

Seedling Lethality ◽

Eukaryotic Organisms

Abstract Background Mitogen-activated protein kinase (MAPK) cascades are conserved signaling modules in eukaryotic organisms and play essential roles in immunity and stress responses. However, the role of MAPKs in chloroplast development remains to be evidently established. Results In this study, a rice chlorosis seedling lethality 1 (csl1) mutant with a Zhonghua11 (ZH11, japonica) background was isolated. Seedlings of the mutant were characterized by chlorotic leaves and death after the trefoil stage, and chloroplasts were observed to contain accumulated starch granules. Molecular cloning revealed that OsCSL1 encoded a MAPK kinase kinase22 (MKKK22) targeted to the endoplasmic reticulum (ER), and functional complementation of OsCSL1 was found to restore the normal phenotype in csl1 plants. The CRISPR/Cas9 technology was used for targeted disruption of OsCSL1, and the OsCSL1-Cas9 lines obtained therein exhibited yellow seedlings which phenocopied the csl1 mutant. CSL1/MKKK22 was observed to establish direct interaction with MKK4, and altered expression of MKK1 and MKK4 was detected in the csl1 mutant. Additionally, disruption of OsCSL1 led to reduced expression of chloroplast-associated genes, including chlorophyll biosynthetic genes, plastid-encoded RNA polymerases, nuclear-encoded RNA polymerase, and nuclear-encoded chloroplast genes. Conclusions The findings of this study revealed that OsCSL1 played roles in regulating the expression of multiple chloroplast synthesis-related genes, thereby affecting their functions, and leading to wide-ranging defects, including chlorotic seedlings and severely disrupted chloroplasts containing accumulated starch granules.

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Comprehensive analysis of mitogen-activated protein kinase cascades in chrysanthemum

PeerJ ◽

10.7717/peerj.5037 ◽

2018 ◽

Vol 6 ◽

pp. e5037 ◽

Cited By ~ 1

Author(s):

Aiping Song ◽

Yueheng Hu ◽

Lian Ding ◽

Xue Zhang ◽

Peiling Li ◽

...

Keyword(s):

Protein Kinase ◽

Expression Patterns ◽

Defense Responses ◽

Mitogen Activated Protein Kinase ◽

Pcr Analysis ◽

Yeast Two Hybrid ◽

Qrt Pcr ◽

Mapk Cascades ◽

Mitogen Activated Protein ◽

Two Hybrid

Background Mitogen-activated protein kinase (MAPK) cascades, an important type of pathway in eukaryotic signaling networks, play a key role in plant defense responses, growth and development. Methods Phylogenetic analysis and conserved motif analysis of the MKK and MPK families in Arabidopsis thaliana, Helianthus annuus and Chrysanthemum morifolium classified MKK genes and MPK genes. qRT-PCR was used for the expression patterns of CmMPK and CmMKK genes, and yeast two-hybrid assay was applied to clear the interaction between CmMPKs and CmMKKs. Results We characterized six MKK genes and 11 MPK genes in chrysanthemum based on transcriptomic sequences and classified these genes into four groups. qRT-PCR analysis demonstrated that CmMKKs and CmMPKs exhibited various expression patterns in different organs of chrysanthemum and in response to abiotic stresses and phytohormone treatments. Furthermore, a yeast two-hybrid assay was applied to analyze the interaction between CmMKKs and CmMPKs and reveal the MAPK cascades in chrysanthemum. Discussion Our data led us to propose that CmMKK4-CmMPK13 and CmMKK2-CmMPK4 may be involved in regulating salt resistance and in the relationship between CmMKK9 and CmMPK6 and temperature stress.

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Exercise-induced mitogen-activated protein kinase signalling in skeletal muscle

Proceedings of The Nutrition Society ◽

10.1079/pns2004346 ◽

2004 ◽

Vol 63 (2) ◽

pp. 227-232 ◽

Cited By ~ 48

Author(s):

Yun Chau Long ◽

Ulrika Widegren ◽

Juleen R. Zierath

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Muscle Contraction ◽

Mitogen Activated Protein Kinase ◽

Mapk Cascades ◽

Extracellular Signal ◽

Mapk Signalling ◽

Mitogen Activated Protein ◽

Exercise Induced ◽

Response To Exercise

Exercise training improves glucose homeostasis through enhanced insulin sensitivity in skeletal muscle. Muscle contraction through physical exercise is a physiological stimulus that elicits multiple biochemical and biophysical responses and therefore requires an appropriate control network. Mitogen-activated protein kinase (MAPK) signalling pathways constitute a network of phosphorylation cascades that link cellular stress to changes in transcriptional activity. MAPK cascades are divided into four major subfamilies, including extracellular signal-regulated kinases 1 and 2, p38 MAPK, c-Jun NH2-terminal kinase and extracellular signal-regulated kinase 5. The present review will present the current understanding of parallel MAPK signalling in human skeletal muscle in response to exercise and muscle contraction, with an emphasis on identifying potential signalling mechanisms responsible for changes in gene expression.

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Protein Kinase A Operates a Molecular Switch That Governs Yeast Pseudohyphal Differentiation

Molecular and Cellular Biology ◽

10.1128/mcb.22.12.3981-3993.2002 ◽

2002 ◽

Vol 22 (12) ◽

pp. 3981-3993 ◽

Cited By ~ 137

Author(s):

Xuewen Pan ◽

Joseph Heitman

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Pathogenic Fungi ◽

Mitogen Activated Protein Kinase ◽

Signaling Cascades ◽

Mitogen Activated Protein ◽

Eukaryotic Organisms ◽

Pseudohyphal Differentiation ◽

Developmental Switch ◽

Kinase A

ABSTRACT The yeast Saccharomyces cerevisiae undergoes a dimorphic filamentous transition in response to nutrient cues that is affected by both mitogen-activated protein kinase and cyclic AMP-protein kinase A signaling cascades. Here two transcriptional regulators, Flo8 and Sfl1, are shown to be the direct molecular targets of protein kinase A. Flo8 and Sfl1 antagonistically control expression of the cell adhesin Flo11 via a common promoter element. Phosphorylation by the protein kinase A catalytic subunit Tpk2 promotes Flo8 binding and activation of the Flo11 promoter and relieves repression by prohibiting dimerization and DNA binding by Sfl1. Our studies illustrate in molecular detail how protein kinase A combinatorially effects a key developmental switch. Similar mechanisms may operate in pathogenic fungi and more complex multicellular eukaryotic organisms.

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Fibroblast growth factors activate mitogen-activated protein kinase pathways to promote migration in ovine trophoblast cells

Reproduction ◽

10.1530/rep-10-0541 ◽

2011 ◽

Vol 141 (5) ◽

pp. 707-714 ◽

Cited By ~ 21

Author(s):

Qi En Yang ◽

Mariana I Giassetti ◽

Alan D Ealy

Keyword(s):

Cell Migration ◽

Growth Factors ◽

Fibroblast Growth Factors ◽

Mitogen Activated Protein Kinase ◽

Fibroblast Growth ◽

Trophoblast Cells ◽

Migratory Activity ◽

Mapk Cascades ◽

Mitogen Activated Protein ◽

Cattle And Sheep

Fibroblast growth factors (FGFs) 2 and FGF10 are uterine- and conceptus-derived factors that mediate trophoblast activities in cattle and sheep. To extend our understanding of how FGFs may control peri-implantation development in ruminants, we determined whether FGF2 and FGF10 impact trophoblast cell migration. Transwell inserts containing 8 μm pores were used to examine whether FGF2 or FGF10 supplementation increased oTr1 cell migration. Supplementation with 0.5 ng/ml FGF2 or FGF10 did not affect oTr1 cell migration number, but exposure to 5 or 50 ng/ml FGF2 or FGF10 increased (P<0.05) oTr1 cell migration when compared with controls. The involvement of specific MAP kinase (MAPK) cascades in mediating this FGF response was examined by using pharmacological inhibitors of specific MAPKs. Western blot analysis indicated that FGF2 and FGF10 increased phosphorylation status of MAPKs 1, 3, 8, 9, and 14. Exposure to specific inhibitors blocked FGF induction of each MAPK. Exposure to inhibitors before supplementation with FGF2 or FGF10 prevented FGF induction of cell migration, indicating that each of these signaling molecules was required for FGF effects. A final series of studies examined whether FGF2 and FGF10 also mediated the migration of a bovine trophoblast line (CT1 cell). Increases in migration were detected in each cell line by supplementing 5 or 50 ng/ml FGF2 or FGF10 (P<0.05). In summary, FGF2 and FGF10 regulate migratory activity of ovine trophoblast cells through MAPK-dependent pathways. These outcomes provide further evidence that FGFs function as mediators of peri-implantation conceptus development in cattle and sheep.

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Genome-wide identification of MAPKKK genes and their response to phytoplasma stress in Chinese jujube (Ziziphus jujuba Mill.)

10.21203/rs.2.9872/v1 ◽

2019 ◽

Author(s):

ZhiGuo Liu ◽

Lixin Wang ◽

Chaoling Xue ◽

Yuetong Chu ◽

Weilin Gao ◽

...

Keyword(s):

Protein Kinase ◽

Expression Profiles ◽

Duplication Event ◽

Kinase Domain ◽

Mitogen Activated Protein Kinase ◽

Chinese Jujube ◽

Mapk Cascades ◽

Mitogen Activated Protein ◽

Phytoplasma Infection ◽

Gene Structures

Abstract Backgrounds Mitogen activated protein kinase (MAPK) cascades play vital roles in signal transduction in response to various biotic and abiotic stresses. In the previous study we have identified 10 ZjMAPKs and 5 ZjMAPKKs in Chinese jujube genome and found some crucial members of ZjMAPKs and ZjMAPKKs might function importantly in the process of phytoplasma infection. But how these ZjMAPKKs were modulated by ZjMAPKKKs during this process is still elusive and little information is known about the MAPKKKs in Chinese jujube. Results In the current study, 56 ZjMAPKKKs were identified in the jujube genome and all of them contain the key S-TKc (serine/threonine protein kinase) domain which distributed in all 12 chromosomes. Phylogenetic analysis showed that these ZjMAPKKKs could be classified into two subfamilies, of which 41 belonged to Raf, and 15 to MEKK subfamily. In addition, the ZjMAPKKKs in each subfamily share the same conserved motifs and gene structures, one pair of ZjMAPKKKs (15/16) was the only tandem duplication event on Chromosome 5. Furthermore, the expression profiles of these MAPKKKs in response to phytoplasma disease were investigated by qPCR. In the three main infected tissues (witches’ broom leaves, phyllody leaves, apparent normal leaves), the ZjMAPKKK26 and 45 were significantly up regulated and the ZjMAPKKK3, 43 and 50 were down regulated. While the ZjMAPKKK4, 10, 25 and 44 were significant highly induced in the sterile cultivated tissues infected by phytoplasma, and the ZjMAPKKK7, 30, 35, 37, 40, 41, 43 and 46 were significantly down regulated. Conclusions The identification and classification analysis of ZjMAPKKKs was firstly reported and some key individual ZjMAPKKKs genes might play essential roles in response to phytoplasma infection. This could provide initial understanding for the mechanism that how the ZjMAPKKKs were involved in jujube - phytoplasma infection.

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Mechanism of short-term ERK activation by electromagnetic fields at mobile phone frequencies

Biochemical Journal ◽

10.1042/bj20061653 ◽

2007 ◽

Vol 405 (3) ◽

pp. 559-568 ◽

Cited By ~ 151

Author(s):

Joseph Friedman ◽

Sarah Kraus ◽

Yirmi Hauptman ◽

Yoni Schiff ◽

Rony Seger

Keyword(s):

Mobile Phone ◽

Electromagnetic Fields ◽

Mobile Phones ◽

Egf Receptor ◽

Nadh Oxidase ◽

Mitogen Activated Protein Kinase ◽

Heparin Binding ◽

Cellular Processes ◽

Mapk Cascades ◽

Mitogen Activated Protein

The exposure to non-thermal microwave electromagnetic fields generated by mobile phones affects the expression of many proteins. This effect on transcription and protein stability can be mediated by the MAPK (mitogen-activated protein kinase) cascades, which serve as central signalling pathways and govern essentially all stimulated cellular processes. Indeed, long-term exposure of cells to mobile phone irradiation results in the activation of p38 as well as the ERK (extracellular-signal-regulated kinase) MAPKs. In the present study, we have studied the immediate effect of irradiation on the MAPK cascades, and found that ERKs, but not stress-related MAPKs, are rapidly activated in response to various frequencies and intensities. Using signalling inhibitors, we delineated the mechanism that is involved in this activation. We found that the first step is mediated in the plasma membrane by NADH oxidase, which rapidly generates ROS (reactive oxygen species). These ROS then directly stimulate MMPs (matrix metalloproteinases) and allow them to cleave and release Hb-EGF [heparin-binding EGF (epidermal growth factor)]. This secreted factor activates the EGF receptor, which in turn further activates the ERK cascade. Thus this study demonstrates for the first time a detailed molecular mechanism by which electromagnetic irradiation from mobile phones induces the activation of the ERK cascade and thereby induces transcription and other cellular processes.

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Mitogen-Activated Protein Kinase, Plants, and Heat Stress

Harsh Environment and Plant Resilience ◽

10.1007/978-3-030-65912-7_13 ◽

2021 ◽

pp. 323-354

Author(s):

Jyotsna Bharti ◽

Sahil ◽

Sahil Mehta ◽

Shaban Ahmad ◽

Baljinder Singh ◽

...

Keyword(s):

Heat Stress ◽

Protein Kinase ◽

Mitogen Activated Protein Kinase ◽

Mitogen Activated Protein

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Leptin is involved in acrosome reaction by facilitating activation of MAPK cascades in the Chinese mitten crab, Eriocheir sinensis

Animal Biology ◽

10.1163/15707563-20191095 ◽

2020 ◽

Vol 70 (1) ◽

pp. 81-95

Author(s):

Qing Li ◽

Haitao Zhao ◽

Lin He ◽

Hongdan Yang ◽

Qun Wang

Keyword(s):

Acrosome Reaction ◽

Calcium Ionophore ◽

Eriocheir Sinensis ◽

Calcium Ionophore A23187 ◽

Mitogen Activated Protein Kinase ◽

Ionophore A23187 ◽

Mapk Cascades ◽

Mitten Crab ◽

Mitogen Activated Protein

Abstract The role of leptin has been documented in several studies, including activated threonine phosphorylation of extracellular signal-regulated kinase (ERK1/2) in the reproduction of rodents and humans. Our previous studies have demonstrated that mitogen-activated protein kinase (MAPK) cascades ERK, P38, and c-Jun N-terminal kinase (JNK) are involved in the spermatogenesis and acrosome reaction of Eriocheir sinensis. Therefore, the aim of this study was to investigate the expression of leptin and its receptor (LepR), and the effect of leptin on MAPK cascades during calcium ionophore A23187-induced spermatozoa acrosome reaction in crabs. Successful western blotting revealed a 16 kDa band for leptin, and 120 kDa and 90 kDa bands for the obese receptor (LepR), respectively, in the tested male reproductive tissues. Both leptin and LepR were localized at the pro-acrosomal vesicle and apical cap (AC) of spermatids, suggesting their role in the subsequent acrosome reaction. Moreover, acrosome reaction can be enhanced by leptin, and this effect decreased due to the anti-LepR antibody. Afterwards, we investigated the effects of leptin on MAPK cascades. The results showed that leptin mainly activated the phosphorylation of ERK, P38 and JNK proteins in the apical cap during the acrosome reaction in crab spermatozoa. This study addresses the role of leptin on spermatozoa, and suggests that leptin may induce molecular changes associated with spermatozoa during acrosome reaction.

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