scholarly journals The Hog1 Mitogen-Activated Protein Kinase Is Essential in the Oxidative Stress Response and Chlamydospore Formation in Candidaalbicans

2003 ◽  
Vol 2 (2) ◽  
pp. 351-361 ◽  
Author(s):  
Rebeca Alonso-Monge ◽  
Federico Navarro-García ◽  
Elvira Román ◽  
Ana I. Negredo ◽  
Blanca Eisman ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Stress Response ◽  
Map Kinase ◽  
Uv Light ◽  
Molecular Model ◽  
Oxidative Stress Response ◽  
Mitogen Activated Protein Kinase ◽  
Chlamydospore Formation ◽  
Mitogen Activated Protein

ABSTRACT Candida albicans mutants with mutations in mitogen-activated protein (MAP) kinase HOG1 displayed an increased sensitivity to agents producing reactive oxygen species, such as oxidants (menadione, hydrogen peroxide, or potassium superoxide), and UV light. Consistent with this finding, C. albicans Hog1 was activated not only in response to an increase in external osmolarity, as happens with its Saccharomyces cerevisiae homologue, but also in response to hydrogen peroxide. The Hog1-mediated response to oxidative stress was different from that of transcription factor Cap1, the homologue of S. cerevisiae Yap1, as shown by the different sensitivities to oxidants and the kinetics of cell death of cap1Δ, hog1, and hog1 cap1Δ mutants. Deletion of CAP1 did not influence the level of Hog1 phosphorylation, and deletion of HOG1 did not affect Cap1 nuclear localization. Moreover, we show that the HOG1 gene plays a role in chlamydospore formation, another oxygen-related morphogenetic event, as demonstrated by the fact that hog1 cells were unable to generate these thick-walled structures in several media through a mechanism different from that of the EFG1 regulator. This is the first demonstration of the role of the Hog1-mediated MAP kinase pathway in resistance to oxidative stress in pathogenic fungi, and it allows us to propose a molecular model for the oxidative stress response in C. albicans.

TheahpDgene ofCorynebacterium glutamicumplays an important role in hydrogen peroxide-induced oxidative stress response

2018 ◽  
Vol 165 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Eun-Ji Hong ◽  
Haeri Jeong ◽  
Dong-Seok Lee ◽  
Younhee Kim ◽  
Heung-Shick Lee
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Stress Response ◽  
Oxidative Stress Response

scholarly journals p38 MAPK links oxidative stress to autophagy-related gene expression in cachectic muscle wasting

2010 ◽  
Vol 298 (3) ◽  
pp. C542-C549 ◽  
Author(s):  
J. M. McClung ◽  
A. R. Judge ◽  
S. K. Powers ◽  
Z. Yan
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Protein Modification ◽  
Muscle Wasting ◽  
Ring Finger ◽  
Mitogen Activated Protein Kinase ◽  
C2c12 Myotubes ◽  
Mitogen Activated Protein ◽  
Ubiquitin Proteasome ◽  
F Box Protein

Oxidative stress is a primary trigger of cachectic muscle wasting, but the signaling pathway(s) that links it to the muscle wasting processes remains to be defined. Here, we report that activation of p38 mitogen-activated protein kinase (MAPK) (phosphorylation) and increased oxidative stress ( trans-4-hydroxy-2-nonenal protein modification) in skeletal muscle occur as early as 8 h after lipopolysaccharide (1 mg/kg) and 24 h after dexamethasone (25 mg/kg) injection (intraperitoneal) in mice, concurrent with upregulation of autophagy-related genes, Atg6, Atg7, and Atg12. Treating cultured C2C12 myotubes with oxidant hydrogen peroxide (4 h) resulted in increased p38 phosphorylation and reduced FoxO3 phosphorylation along with induced Atg7 mRNA expression without activation of NF-κ B or FoxO3a transcriptional activities. Furthermore, inhibition of p38α/β by SB202190 blocked hydrogen peroxide-induced atrophy with diminished upregulation of Atg7 and atrogenes [muscle atrophy F-box protein ( MAFbx/Atrogin-1) , muscle ring finger protein 1 ( MuRF-1), and Nedd4]. These findings provide direct evidence for p38α/β MAPK in mediating oxidative stress-induced autophagy-related genes, suggesting that p38α/β MAPK regulates both the ubiquitin-proteasome and the autophagy-lysosome systems in muscle wasting.

Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A

2001 ◽  
Vol 359 (3) ◽  
pp. 497-505 ◽  
Author(s):  
Sunke HIMPEL ◽  
Pascal PANZER ◽  
Klaus EIRMBTER ◽  
Hanna CZAJKOWSKA ◽  
Muhammed SAYED ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Mammalian Cells ◽  
Catalytic Domain ◽  
Molecular Model ◽  
Enzymic Activity ◽  
Mitogen Activated Protein Kinase ◽  
Kinase Family ◽  
Extracellular Signal ◽  
Mitogen Activated Protein

Protein kinases of the DYRK (‘dual-specificity tyrosine-regulated kinase’) family are characterized by a conserved Tyr-Xaa-Tyr motif (Tyr-319–Tyr-321) in a position exactly corresponding to the activation motif of the mitogen-activated protein kinase (MAP kinase) family (Thr-Xaa-Tyr). In a molecular model of the catalytic domain of DYRK1A, the orientation of phosphorylated Tyr-321 is strikingly similar to that of Tyr-185 in the known structure of the activated MAP kinase, extracellular-signal-regulated kinase 2. Consistent with our model, substitution of Tyr-321 but not of Tyr-319 by phenylalanine markedly reduced the enzymic activity of recombinant DYRK1A expressed in either Escherichia coli or mammalian cells. Direct identification of phosphorylated residues by tandem MS confirmed that Tyr-321, but not Tyr-319, was phosphorylated. When expressed in COS-7 cells, DYRK1A was found to be fully phosphorylated on Tyr-321. A catalytically inactive mutant of DYRK1A contained no detectable phosphotyrosine, indicating that Tyr-321 is autophosphorylated by DYRK1A. MS identified Tyr-111 and Ser-97 as additional autophosphorylation sites in the non-catalytic N-terminal domain of bacterially expressed DYRK1A. Enzymic activity was not affected in the DYRK1A-Y111F mutant. The present experimental data and the molecular model indicate that the activity of DYRK1A is dependent on the autophosphorylation of a conserved tyrosine residue in the activation loop.

scholarly journals Oxidative stress response ofInonotus obliquusinduced by hydrogen peroxide

2009 ◽  
Vol 47 (8) ◽  
pp. 814-823 ◽  
Author(s):  
Weifa Zheng ◽  
Yanxia Zhao ◽  
Meimei Zhang ◽  
Zhiwen Wei ◽  
Kangjie Miao ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Stress Response ◽  
Oxidative Stress Response

Oxidative stress response of Inonotus obliquus induced by hydrogen peroxide

2009 ◽  
pp. 1-10 ◽  
Author(s):  
Weifa Zheng ◽  
Yanxia Zhao ◽  
Meimei Zhang ◽  
Zhiwen Wei ◽  
Kangjie Miao ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Stress Response ◽  
Oxidative Stress Response ◽  
Inonotus Obliquus
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