scholarly journals The Dual-Specificity Protein Phosphatase Yvh1p Acts Upstream of the Protein Kinase Mck1p in Promoting Spore Development in Saccharomyces cerevisiae

1999 ◽  
Vol 181 (17) ◽  
pp. 5219-5224 ◽  
Author(s):  
Alexander E. Beeser ◽  
Terrance G. Cooper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Phosphatase ◽  
Vegetative Growth ◽  
Nitrogen Starvation ◽  
Developmental Pathway ◽  
Dual Specificity ◽  
Dual Specificity Protein Phosphatase ◽  
Specificity Protein ◽  
Spore Maturation

ABSTRACT Diploid Saccharomyces cerevisiae cells induce YVH1 expression and enter the developmental pathway, leading to sporulation when starved for nitrogen. We show that yvh1 disruption causes a defect in spore maturation; overexpression of MCK1or IME1 suppresses this yvh1 phenotype. Whilemck1 mutations are epistatic to those in yvh1relative to spore maturation, overexpression of MCK1 does not suppress the yvh1 slow-vegetative-growth phenotype. We conclude that (i) Yvh1p functions earlier than Mck1p and Ime1p in the signal transduction cascade that regulates sporulation and is triggered by nitrogen starvation and (ii) the role of Yvh1p in gametogenesis can be genetically distinguished from its role in vegetative growth.

scholarly journals Immunohistochemical Expression of Dual-Specificity Protein Phosphatase 4 in Patients with Colorectal Adenocarcinoma

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Jongmin Sim ◽  
Kijong Yi ◽  
Hyunsung Kim ◽  
Hyein Ahn ◽  
Yumin Chung ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Colorectal Adenocarcinoma ◽  
Malignant Tumors ◽  
Male Gender ◽  
Rank Test ◽  
Log Rank Test ◽  
Dual Specificity ◽  
Dual Specificity Protein Phosphatase ◽  
Specificity Protein

The role of dual-specificity protein phosphatase 4 (DUSP4) appears to vary with the type of malignant tumors and is still controversial. The purpose of our study was to clarify the exact role of DUSP4 expression in colorectal adenocarcinoma. We constructed tissue microarrays and investigated DUSP4 expression by immunohistochemistry. DUSP4 was more frequently expressed in adenocarcinomas and lymph node/distant metastases compared to that in normal colorectal tissues and tubular adenomas (P<0.001). Mean DUSP4 expression score was significantly higher in malignant tumors than in benign lesions (P<0.001). DUSP4 expression was significantly correlated with older age (P=0.017), male gender (P=0.036), larger tumor size (P=0.014), nonmucinous tumor type (P=0.023), and higher T stage (P=0.040). Kaplan-Meier survival curves revealed a significant effect of DUSP4 expression on both overall survival and disease-free survival in AJCC stage I (P=0.008andP=0.003, resp., log-rank test) and male gender (P=0.017andP=0.049, resp., log-rank test). DUSP4 protein is frequently upregulated in colorectal adenocarcinoma and may play an important role in carcinogenesis and cancer progression and may be a marker of adverse prognosis.

scholarly journals Role of dual-specificity protein phosphatase-5 in modulating the myogenic response in rat cerebral arteries

2013 ◽  
Vol 114 (2) ◽  
pp. 252-261 ◽  
Author(s):  
Nadi T. Wickramasekera ◽  
Debebe Gebremedhin ◽  
Koryn A. Carver ◽  
Padmanabhan Vakeel ◽  
Ramani Ramchandran ◽  
...  
Keyword(s):  
Protein Expression ◽  
Protein Phosphatase ◽  
Single Channel ◽  
Cerebral Arteries ◽  
Protein Phosphatase 5 ◽  
Dual Specificity ◽  
Arterial Constriction ◽  
Dual Specificity Protein Phosphatase ◽  
Specificity Protein

The present study examined the role of the dual-specificity protein phosphatase-5 (DUSP-5) in the pressure-induced myogenic responses of organ-cultured cerebral arterial segments. In these studies, we initially compared freshly isolated and organ-cultured cerebral arterial segments with respect to responses to step increases in intravascular pressure, vasodilator and vasoconstrictor stimuli, activities of the large-conductance arterial Ca2+-activated K+ (KCa) single-channel current, and stable protein expression of DUSP-5 enzyme. The results demonstrate maintained pressure-dependent myogenic vasoconstriction, DUSP-5 protein expression, endothelium-dependent and -independent dilations, agonist-induced constriction, and unitary KCa channel conductance in organ-cultured cerebral arterial segments similar to that in freshly isolated cerebral arteries. Furthermore, using a permeabilization transfection technique in organ-cultured cerebral arterial segments, gene-specific small interfering RNA (siRNA) induced knockdown of DUSP-5 mRNA and protein, which were associated with enhanced pressure-dependent cerebral arterial myogenic constriction and increased phosphorylation of PKC-βII. In addition, siRNA knockdown of DUSP-5 reduced levels of phosphorylated ROCK and ERK1 with no change in the level of phosphorylated ERK2. Pharmacological inhibition of ERK1/2 phosphorylation significantly attenuated pressure-induced myogenic constriction in cerebral arteries. The findings within the present studies illustrate that DUSP-5, native in cerebral arterial muscle cells, appears to regulate signaling of pressure-dependent myogenic cerebral arterial constriction, which is crucial for the maintenance of constant cerebral blood flow to the brain.

scholarly journals Genome-scale comparative analysis for host resistance against sea lice between Atlantic salmon and rainbow trout

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Pablo Cáceres ◽  
Agustín Barría ◽  
Kris A. Christensen ◽  
Liane N. Bassini ◽  
Katharina Correa ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Atlantic Salmon ◽  
Candidate Genes ◽  
Protein Phosphatase ◽  
Sea Lice ◽  
Genome Wide Association Studies ◽  
Dual Specificity ◽  
Dual Specificity Protein Phosphatase ◽  
Genomic Regions ◽  
Specificity Protein

AbstractSea lice (Caligus rogercresseyi) is an ectoparasite which causes major production losses in the salmon aquaculture industry worldwide. Atlantic salmon (Salmo salar) and rainbow trout (Oncorhynchus mykiss) are two of the most susceptible salmonid species to sea lice infestation. The objectives of this study were to: (1) identify genomic regions associated with resistance to Caligus rogercresseyi in Atlantic salmon and rainbow trout by performing single-step Genome-Wide Association studies (ssGWAS), and (2) identify candidate genes related to trait variation based on exploring orthologous genes within the associated regions across species. A total of 2626 Atlantic salmon and 2643 rainbow trout were challenged and genotyped with 50 K and 57 K SNP panels, respectively. We ran two independent ssGWAS for sea lice resistance on each species and identified 7 and 13 regions explaining more than 1% of the genetic variance for the trait, with the most important regions explaining 3% and 2.7% for Atlantic salmon and rainbow trout, respectively. We identified genes associated with immune response, cytoskeleton function, and cell migration when focusing on important genomic regions for each species. Moreover, we found 15 common orthogroups which were present in more than one associated genomic region, within- or between-species; however, only one orthogroup showed a clear potential biological relevance in the response against sea lice. For instance, dual-specificity protein phosphatase 10-like (dusp10) and dual-specificity protein phosphatase 8 (dusp8) were found in genomic regions associated with lice density in Atlantic salmon and rainbow trout, respectively. Dusp10 and dusp8 are modulators of the MAPK pathway and might be involved in the differences of the inflammation response between lice resistant and susceptible fish from both species. Our results provide further knowledge on candidate genes related to sea lice resistance and may help establish better control for sea lice in fish populations.

Dual-specificity protein phosphatase Msg5 controls cell wall integrity and virulence in Fusarium oxysporum

2021 ◽  
Vol 146 ◽  
pp. 103486
Author(s):  
Tânia R. Fernandes ◽  
Encarnación Sánchez Salvador ◽  
Ángela G. Tapia ◽  
Antonio Di Pietro
Keyword(s):  
Cell Wall ◽  
Fusarium Oxysporum ◽  
Protein Phosphatase ◽  
Cell Wall Integrity ◽  
Dual Specificity ◽  
Dual Specificity Protein Phosphatase ◽  
Specificity Protein
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