scholarly journals Global Analysis of Serine-Threonine Protein Kinase Genes in Neurospora crassa

2011 ◽  
Vol 10 (11) ◽  
pp. 1553-1564 ◽  
Author(s):  
Gyungsoon Park ◽  
Jacqueline A. Servin ◽  
Gloria E. Turner ◽  
Lorena Altamirano ◽  
Hildur V. Colot ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Neurospora Crassa ◽  
Growth And Development ◽  
Global Analysis ◽  
Large Fraction ◽  
Kinase Gene ◽  
Content Type ◽  
Chemical Screening ◽  
Chemical Treatments ◽  
Total Percentage

ABSTRACTSerine/threonine (S/T) protein kinases are crucial components of diverse signaling pathways in eukaryotes, including the model filamentous fungusNeurospora crassa. In order to assess the importance of S/T kinases toNeurosporabiology, we embarked on a global analysis of 86 S/T kinase genes inNeurospora. We were able to isolate viable mutants for 77 of the 86 kinase genes. Of these, 57% exhibited at least one growth or developmental phenotype, with a relatively large fraction (40%) possessing a defect in more than one trait. S/T kinase knockouts were subjected to chemical screening using a panel of eight chemical treatments, with 25 mutants exhibiting sensitivity or resistance to at least one chemical. This brought the total percentage of S/T mutants with phenotypes in our study to 71%. Mutants lackingapg-1, an S/T kinase required for autophagy in other organisms, possessed the greatest number of phenotypes, with defects in asexual and sexual growth and development and in altered sensitivity to five chemical treatments. We showed that NCU02245/stk-19is required for chemotropic interactions between female and male cells during mating. Finally, we demonstrated allelism between the S/T kinase gene NCU00406 andvelvet(vel), encoding a p21-activated protein kinase (PAK) gene important for asexual and sexual growth and development inNeurospora.

scholarly journals Circadian Activation of the Mitogen-Activated Protein Kinase MAK-1 Facilitates Rhythms in Clock-Controlled Genes in Neurospora crassa

2012 ◽  
Vol 12 (1) ◽  
pp. 59-69 ◽  
Author(s):  
Lindsay D. Bennett ◽  
Phillip Beremand ◽  
Terry L. Thomas ◽  
Deborah Bell-Pedersen
Keyword(s):  
Protein Kinase ◽  
Circadian Clock ◽  
Neurospora Crassa ◽  
Cellular Growth ◽  
Mitogen Activated Protein Kinase ◽  
Content Type ◽  
Cell Wall Integrity Pathway ◽  
Wide Range ◽  
Mitogen Activated Protein ◽  
Significant Enrichment

ABSTRACTThe circadian clock regulates the expression of many genes involved in a wide range of biological functions through output pathways such as mitogen-activated protein kinase (MAPK) pathways. We demonstrate here that the clock regulates the phosphorylation, and thus activation, of the MAPKs MAK-1 and MAK-2 in the filamentous fungusNeurospora crassa. In this study, we identified genetic targets of the MAK-1 pathway, which is homologous to the cell wall integrity pathway inSaccharomyces cerevisiaeand the extracellular signal-regulated kinase 1/2 (ERK1/2) pathway in mammals. When MAK-1 was deleted fromNeurosporacells, vegetative growth was reduced and the transcript levels for over 500 genes were affected, with significant enrichment for genes involved in protein synthesis, biogenesis of cellular components, metabolism, energy production, and transcription. Additionally, of the ∼500 genes affected by the disruption of MAK-1, more than 25% were previously identified as putative clock-controlled genes. We show that MAK-1 is necessary for robust rhythms of two morning-specific genes, i.e.,ccg-1and the mitochondrial phosphate carrier protein gene NCU07465. Additionally, we show clock regulation of a predicted chitin synthase gene, NCU04352, whose rhythmic accumulation is also dependent upon MAK-1. Together, these data establish a role for the MAK-1 pathway as an output pathway of the circadian clock and suggest a link between rhythmic MAK-1 activity and circadian control of cellular growth.

Characterization of a protein kinase gene from two Chlorella viruses

1995 ◽  
Vol 35 (3) ◽  
pp. 291-305 ◽  
Author(s):  
Quideng Que ◽  
James L. Van Etten
Keyword(s):  
Protein Kinase ◽  
Kinase Gene ◽  
Protein Kinase Gene

scholarly journals Direct evidence for a key role of protein kinase C in the development of vasospasm after subarachnoid hemorrhage

1992 ◽  
Vol 76 (4) ◽  
pp. 635-639 ◽  
Author(s):  
Shigeru Nishizawa ◽  
Nobukazu Nezu ◽  
Kenichi Uemura
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Direct Evidence ◽  
Control Group ◽  
Content Type ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Fine Print

✓ Vascular contraction is induced by the activation of intracellular contractile proteins mediated through signal transduction from the outside to the inside of cells. Protein kinase C plays a crucial role in this signal transduction. It is hypothesized that protein kinase C plays a causative part in the development of vasospasm after subarachnoid hemorrhage (SAH). To verify this directly, the authors measured protein kinase C activity in canine basilar arteries in an SAH model with (γ-32P)adenosine triphosphate and the data were compared to those in a control group. Protein kinase C is translocated to the membrane from the cytosol when it is activated, and the translocation is an index of the activation; thus, protein kinase C activity was measured both in the cytosol and in the membrane fractions. Protein kinase C activity in the membrane in the SAH model was remarkably enhanced compared to that in the control group. The percentage of membrane activity to the total was also significantly greater in the SAH vessels than in the control group, and the percentage of cytosol activity in the SAH group was decreased compared to that in the control arteries. The results indicate that protein kinase C in the vascular smooth muscle was translocated to the membrane from the cytosol and was activated when SAH occurred. It is concluded that this is direct evidence for a key role of protein kinase C in the development of vasospasm.

scholarly journals The Evolutionary History and Diverse Physiological Roles of the Grapevine Calcium-Dependent Protein Kinase Gene Family

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e80818 ◽  
Author(s):  
Fei Chen ◽  
Marianna Fasoli ◽  
Giovanni Battista Tornielli ◽  
Silvia Dal Santo ◽  
Mario Pezzotti ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Gene Family ◽  
Evolutionary History ◽  
Dependent Protein Kinase ◽  
Kinase Gene ◽  
Calcium Dependent ◽  
Dependent Protein ◽  
Protein Kinase Gene ◽  
Calcium Dependent Protein Kinase

scholarly journals Coxiella burnetii Alters Cyclic AMP-Dependent Protein Kinase Signaling during Growth in Macrophages

2012 ◽  
Vol 80 (6) ◽  
pp. 1980-1986 ◽  
Author(s):  
Laura J. MacDonald ◽  
Richard C. Kurten ◽  
Daniel E. Voth
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Coxiella Burnetii ◽  
Alveolar Macrophages ◽  
Q Fever ◽  
Parasitophorous Vacuole ◽  
Dependent Protein Kinase ◽  
Content Type ◽  
Bacterial Agent ◽  
Dependent Protein

ABSTRACTCoxiella burnetiiis the bacterial agent of human Q fever, an acute, flu-like illness that can present as chronic endocarditis in immunocompromised individuals. Following aerosol-mediated transmission,C. burnetiireplicates in alveolar macrophages in a unique phagolysosome-like parasitophorous vacuole (PV) required for survival. The mechanisms ofC. burnetiiintracellular survival are poorly defined and a recent Q fever outbreak in the Netherlands emphasizes the need for better understanding this unique host-pathogen interaction. We recently demonstrated that inhibition of host cyclic AMP-dependent protein kinase (PKA) activity negatively impacts PV formation. In the current study, we confirmed PKA involvement in PV biogenesis and probed the role of PKA signaling duringC. burnetiiinfection of macrophages. Using PKA-specific inhibitors, we found the kinase was needed for biogenesis of prototypical PV andC. burnetiireplication. PKA and downstream targets were differentially phosphorylated throughout infection, suggesting prolonged regulation of the pathway. Importantly, the pathogen actively triggered PKA activation, which was also required for PV formation by virulentC. burnetiiisolates during infection of primary human alveolar macrophages. A subset of PKA-specific substrates were differentially phosphorylated duringC. burnetiiinfection, suggesting the pathogen uses PKA signaling to control distinct host cell responses. Collectively, the current results suggest a versatile role for PKA inC. burnetiiinfection and indicate virulent organisms usurp host kinase cascades for efficient intracellular growth.

Sign in / Sign up

Export Citation Format

Share Document