Signal integration in budding yeast

2010 ◽  
Vol 38 (5) ◽  
pp. 1257-1264 ◽  
Author(s):  
Christian Waltermann ◽  
Edda Klipp
Keyword(s):  
Morphological Differentiation ◽  
Quantitative Model ◽  
Mitogen Activated Protein Kinase ◽  
Signal Integration ◽  
High Osmolarity Glycerol ◽  
Signalling Network ◽  
Mitogen Activated Protein ◽  
Integration Mechanisms ◽  
Protein Kinase Signalling ◽  
Growth Ph

A complex signalling network governs the response of Saccharomyces cerevisiae to an array of environmental stimuli and stresses. In the present article, we provide an overview of the main signalling system and discuss the mechanisms by which yeast integrates and separates signals from these sources. We apply our classification scheme to a simple semi-quantitative model of the HOG (high-osmolarity glycerol)/FG (filamentous growth)/PH (pheromone) MAPK (mitogen-activated protein kinase) signalling network by perturbing its signal integration mechanisms under combinatorial stimuli of osmotic stress, starvation and pheromone exposure in silico. Our findings include that the Hog1 MAPK might act as a timer for filamentous differentiation, not allowing morphological differentiation before osmo-adaptation is sufficiently completed. We also see that a mutually exclusive decision-making between pheromone and osmo-response might not be taken on the MAPK level and transcriptional regulation of MAPK targets. We conclude that signal integration mechanisms in a wider network including the cell cycle have to be taken into account for which our framework might provide focal points of study.

The JIP family of MAPK scaffold proteins

2006 ◽  
Vol 34 (5) ◽  
pp. 828-832 ◽  
Author(s):  
A.J. Whitmarsh
Keyword(s):  
Cell Function ◽  
Biochemical Properties ◽  
Scaffold Proteins ◽  
Mitogen Activated Protein Kinase ◽  
Signal Integration ◽  
Mapk Signalling ◽  
Mitogen Activated Protein ◽  
Β Cell Function ◽  
Insulin Responses ◽  
Protein Kinase Signalling

The components of MAPK (mitogen-activated protein kinase) signalling pathways can assemble into complexes that are co-ordinated by regulatory proteins including scaffold proteins. There is increasing evidence that scaffold proteins (i) maintain signalling specificity and facilitate the activation of pathway components, (ii) localize pathway components to particular subcellular sites or to specific targets, and (iii) serve as a point of signal integration to allow regulation of MAPK pathways by other signalling events in the cell. One family of scaffold proteins that regulate signalling by stress-activated MAPKs are the JIPs [JNK (c-Jun N-terminal kinase)-interacting proteins]. JIP proteins have been demonstrated to form complexes with specific JNK and p38 MAPK signalling modules and to play important roles in brain development, neuronal trafficking, apoptosis, β-cell function and insulin responses. Here, I briefly review our current understanding of the biochemical properties and physiological roles of JIP proteins.

Involvement of mitogen-activated protein kinase signalling in pearl millet–downy mildew interaction

Plant Science ◽  
2014 ◽  
Vol 214 ◽  
pp. 29-37 ◽  
Author(s):  
Prasad Melvin ◽  
Sreedhara Ashok Prabhu ◽  
Chandra Pal Anup ◽  
Sekhar Shailasree ◽  
Huntrike Shekar Shetty ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Downy Mildew ◽  
Pearl Millet ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Protein Kinase Signalling

scholarly journals Whey protein concentrate enhances intestinal integrity and influences transforming growth factor-β1 and mitogen-activated protein kinase signalling pathways in piglets after lipopolysaccharide challenge

2016 ◽  
Vol 115 (6) ◽  
pp. 984-993 ◽  
Author(s):  
Kan Xiao ◽  
Lefei Jiao ◽  
Shuting Cao ◽  
Zehe Song ◽  
Caihong Hu ◽  
...  
Keyword(s):  
Transforming Growth Factor ◽  
Intestinal Inflammation ◽  
Control Diet ◽  
Intestinal Barrier ◽  
Mitogen Activated Protein Kinase ◽  
Whey Protein Concentrate ◽  
Protective Effects ◽  
Mitogen Activated Protein ◽  
And Control ◽  
Protein Kinase Signalling

AbstractWhey protein concentrate (WPC) has been reported to have protective effects on the intestinal barrier. However, the molecular mechanisms involved are not fully elucidated. Transforming growth factor-β1 (TGF-β1) is an important component in the WPC, but whether TGF-β1 plays a role in these processes is not clear. The aim of this study was to investigate the protective effects of WPC on the intestinal epithelial barrier as well as whether TGF-β1 is involved in these protection processes in a piglet model after lipopolysaccharide (LPS) challenge. In total, eighteen weanling pigs were randomly allocated to one of the following three treatment groups: (1) non-challenged control and control diet; (2) LPS-challenged control and control diet; (3) LPS+5 %WPC diet. After 19 d of feeding with control or 5 %WPC diets, pigs were injected with LPS or saline. At 4 h after injection, pigs were killed to harvest jejunal samples. The results showed that WPC improved (P<0·05) intestinal morphology, as indicated by greater villus height and villus height:crypt depth ratio, and intestinal barrier function, which was reflected by increased transepithelial electrical resistance and decreased mucosal-to-serosal paracellular flux of dextran (4 kDa), compared with the LPS group. Moreover, WPC prevented the LPS-induced decrease (P<0·05) in claudin-1, occludin and zonula occludens-1 expressions in the jejunal mucosae. WPC also attenuated intestinal inflammation, indicated by decreased (P<0·05) mRNA expressions of TNF-α, IL-6, IL-8 and IL-1β. Supplementation with WPC also increased (P<0·05) TGF-β1 protein, phosphorylated-Smad2 expression and Smad4 and Smad7 mRNA expressions and decreased (P<0·05) the ratios of the phosphorylated to total c-jun N-terminal kinase (JNK) and p38 (phospho-JNK:JNK and p-p38:p38), whereas it increased (P<0·05) the ratio of extracellular signal-regulated kinase (ERK) (phospho-ERK:ERK). Collectively, these results suggest that dietary inclusion of WPC attenuates the LPS-induced intestinal injury by improving mucosal barrier function, alleviating intestinal inflammation and influencing TGF-β1 canonical Smad and mitogen-activated protein kinase signalling pathways.

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