W55aEncodes a Novel Protein Kinase That Is Involved in Multiple Stress Responses

Mitogen-activated protein kinase (MAPK) cascades are the universal signal transduction networks that regulate cell growth and development, hormone signaling, and other environmental stresses. However, their essential contribution to plant tolerance is very little known in the potato (Solanum tuberosum) plant. The current study carried out a genome-wide study of StMAPK and provided a deep insight using bioinformatics tools. In addition, the relative expression of StMAPKs was also assessed in different plant tissues. The similarity search results identified a total of 22 StMAPK genes in the potato genome. The sequence alignment also showed conserved motif TEY/TDY in most StMAPKs with conserved docking LHDXXEP sites. The phylogenetic analysis divided all 22 StMAPK genes into five groups, i.e., A, B, C, D, and E, showing some common structural motifs. In addition, most of the StMAPKs were found in a cluster form at the terminal of chromosomes. The promoter analysis predicted several stress-responsive Cis-acting regulatory elements in StMAPK genes. Gene duplication under selection pressure also indicated several purifying and positive selections in StMAPK genes. In potato, StMAPK2, StMAPK6, and StMAPK19 showed a high expression in response to heat stress. Under ABA and IAA treatment, the expression of the total 20 StMAPK genes revealed that ABA and IAA played an essential role in this defense process. The expression profiling and real-time qPCR (RT-qPCR) exhibited their high expression in roots and stems compared to leaves. These results deliver primary data for functional analysis and provide reference data for other important crops.

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Puumala and Andes Orthohantaviruses Cause Transient Protein Kinase R-Dependent Formation of Stress Granules

Journal of Virology ◽

10.1128/jvi.01168-19 ◽

2019 ◽

Vol 94 (3) ◽

Cited By ~ 4

Author(s):

Wanda Christ ◽

Janne Tynell ◽

Jonas Klingström

Keyword(s):

Protein Kinase ◽

Host Cell ◽

Stress Responses ◽

Stress Granules ◽

Cell Stress ◽

Stress Granule ◽

Hantavirus Infection ◽

Stress Signaling ◽

Protein Kinase R ◽

Granule Formation

ABSTRACT Virus infection frequently triggers host cell stress signaling resulting in translational arrest; as a consequence, many viruses employ means to modulate the host stress response. Hantaviruses are negative-sense, single-stranded RNA viruses known to inhibit host innate immune responses and apoptosis, but their impact on host cell stress signaling remains largely unknown. In this study, we investigated activation of host cell stress responses during hantavirus infection. We show that hantavirus infection causes transient formation of stress granules (SGs) but does so in only a limited proportion of infected cells. Our data indicate some cell type-specific and hantavirus species-specific variability in SG prevalence and show SG formation to be dependent on the activation of protein kinase R (PKR). Hantavirus infection inhibited PKR-dependent SG formation, which could account for the transient nature and low prevalence of SG formation observed during hantavirus infection. In addition, we report only limited colocalization of hantaviral proteins or RNA with SGs and show evidence indicating hantavirus-mediated inhibition of PKR-like endoplasmic reticulum (ER) kinase (PERK). IMPORTANCE Our work presents the first report on stress granule formation during hantavirus infection. We show that hantavirus infection actively inhibits stress granule formation, thereby escaping the detrimental effects on global translation imposed by host stress signaling. Our results highlight a previously uncharacterized aspect of hantavirus-host interactions with possible implications for how hantaviruses are able to cause persistent infection in natural hosts and for pathogenesis.

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Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoforms

The International Journal of Biochemistry & Cell Biology ◽

10.1016/j.biocel.2005.09.001 ◽

2005 ◽

Cited By ~ 4

Author(s):

A ANDREEVA ◽

J PIONTEK ◽

I BLASIG ◽

D UTEPBERGENOV

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Tight Junction ◽

Kinase C ◽

Protein Kinase C Isoforms ◽

Novel Protein

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Physiological Role for Phosphatidic Acid in the Translocation of the Novel Protein Kinase C Apl II in Aplysia Neurons

Molecular and Cellular Biology ◽

10.1128/mcb.00178-08 ◽

2008 ◽

Vol 28 (15) ◽

pp. 4719-4733 ◽

Cited By ~ 17

Author(s):

Carole A. Farah ◽

Ikue Nagakura ◽

Daniel Weatherill ◽

Xiaotang Fan ◽

Wayne S. Sossin

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Phosphatidic Acid ◽

Physiological Role ◽

C2 Domain ◽

The Novel ◽

Physiological Conditions ◽

Kinase C ◽

Neuronal Membranes ◽

Novel Protein

ABSTRACT In Aplysia californica, the serotonin-mediated translocation of protein kinase C (PKC) Apl II to neuronal membranes is important for synaptic plasticity. The orthologue of PKC Apl II, PKCε, has been reported to require phosphatidic acid (PA) in conjunction with diacylglycerol (DAG) for translocation. We find that PKC Apl II can be synergistically translocated to membranes by the combination of DAG and PA. We identify a mutation in the C1b domain (arginine 273 to histidine; PKC Apl II-R273H) that removes the effects of exogenous PA. In Aplysia neurons, the inhibition of endogenous PA production by 1-butanol inhibited the physiological translocation of PKC Apl II by serotonin in the cell body and at the synapse but not the translocation of PKC Apl II-R273H. The translocation of PKC Apl II-R273H in the absence of PA was explained by two additional effects of this mutation: (i) the mutation removed C2 domain-mediated inhibition, and (ii) the mutation decreased the concentration of DAG required for PKC Apl II translocation. We present a model in which, under physiological conditions, PA is important to activate the novel PKC Apl II both by synergizing with DAG and removing C2 domain-mediated inhibition.

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