The MAPKK FgMkk1 ofFusarium graminearumregulates vegetative differentiation, multiple stress response, and virulence via the cell wall integrity and high-osmolarity glycerol signaling pathways

2013 ◽  
Vol 16 (7) ◽  
pp. 2023-2037 ◽  
Author(s):  
Yingzi Yun ◽  
Zunyong Liu ◽  
Jingze Zhang ◽  
Won-Bo Shim ◽  
Yun Chen ◽  
...  
Yeast ◽  
2010 ◽  
Vol 27 (8) ◽  
pp. 495-502 ◽  
Author(s):  
Jose Manuel Rodríguez-Peña ◽  
Raúl García ◽  
César Nombela ◽  
Javier Arroyo

2021 ◽  
Vol 22 (12) ◽  
pp. 6169
Author(s):  
Yunying Zhao ◽  
Shiyun Li ◽  
Jing Wang ◽  
Yingli Liu ◽  
Yu Deng

Cadmium is a carcinogen that can induce ER stress, DNA damage, oxidative stress and cell death. The yeast mitogen-activated protein kinase (MAPK) signalling pathways paly crucial roles in response to various stresses. Here, we demonstrate that the unfolded protein response (UPR) pathway, the high osmolarity glycerol (HOG) pathway and the cell wall integrity (CWI) pathway are all essential for yeast cells to defend against the cadmium-induced toxicity, including the elevated ROS and cell death levels induced by cadmium. We show that the UPR pathway is required for the cadmium-induced phosphorylation of HOG_MAPK Hog1 but not for CWI_MAPK Slt2, while Slt2 but not Hog1 is required for the activation of the UPR pathway through the transcription factors of Swi6 and Rlm1. Moreover, deletion of HAC1 and IRE1 could promote the nuclear accumulation of Hog1, and increase the cytosolic and bud neck localisation of Slt2, indicating crucial roles of Hog1 and Slt2 in regulating the cellular process in the absence of UPR pathway. Altogether, our findings highlight the significance of these two MAPK pathways of HOG and CWI and their interrelationship with the UPR pathway in responding to cadmium-induced toxicity in budding yeast.


2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Raúl García ◽  
Enrique Bravo ◽  
Sonia Diez-Muñiz ◽  
Cesar Nombela ◽  
Jose M. Rodríguez-Peña ◽  
...  

2003 ◽  
Vol 161 (6) ◽  
pp. 1035-1040 ◽  
Author(s):  
Vladimír Reiser ◽  
Desmond C. Raitt ◽  
Haruo Saito

Very little is known about how cellular osmosensors monitor changes in osmolarity of the environment. Here, we report that in yeast, Sln1 osmosensor histidine kinase monitors changes in turgor pressures. Reductions in turgor caused by either hyperosmotic stress, nystatin, or removal of cell wall activate MAPK Hog1 specifically through the SLN1 branch, but not through the SHO1 branch of the high osmolarity glycerol pathway. The integrity of the periplasmic region of Sln1 was essential for its sensor function. We found that activity of the plant histidine kinase cytokinin response 1 (Cre1) is also regulated by changes in turgor pressure, in a manner identical to that of Sln1, in the presence of cytokinin. We propose that Sln1 and Cre1 are turgor sensors, and that similar turgor-sensing mechanisms might regulate hyperosmotic stress responses both in yeast and plants.


Sign in / Sign up

Export Citation Format

Share Document