Induction of a Ribotoxic Stress Response That Stimulates Stress-Activated Protein Kinases by 13-Deoxytedanolide, an Antitumor Marine Macrolide

2006 ◽  
Vol 70 (1) ◽  
pp. 161-171 ◽  
Author(s):  
Kun-Hyung LEE ◽  
Shinichi NISHIMURA ◽  
Shigeki MATSUNAGA ◽  
Nobuhiro FUSETANI ◽  
Hidenori ICHIJO ◽  
...  
Keyword(s):  
Stress Response ◽  
Protein Kinases ◽  
Ribotoxic Stress Response

scholarly journals Activation of the Classical Mitogen-Activated Protein Kinases Is Part of the Shiga Toxin-Induced Ribotoxic Stress Response and May Contribute to Shiga Toxin-Induced Inflammation

2015 ◽  
Vol 84 (1) ◽  
pp. 138-148 ◽  
Author(s):  
Dakshina M. Jandhyala ◽  
Amrita Ahluwalia ◽  
Jennifer J. Schimmel ◽  
Arlin B. Rogers ◽  
John M. Leong ◽  
...  
Keyword(s):  
Stress Response ◽  
Protein Kinases ◽  
Shiga Toxin ◽  
Severe Disease ◽  
Cell Types ◽  
Second Phase ◽  
Mitogen Activated Protein Kinases ◽  
Shiga Toxins ◽  
Ribotoxic Stress Response ◽  
Mitogen Activated Protein

Infection with enterohemorrhagicEscherichia coli(EHEC) can result in severe disease, including hemorrhagic colitis and the hemolytic uremic syndrome. Shiga toxins (Stx) are the key EHEC virulence determinant contributing to severe disease. Despite inhibiting protein synthesis, Shiga toxins paradoxically induce the expression of proinflammatory cytokines from various cell typesin vitro, including intestinal epithelial cells (IECs). This effect is mediated in large part by the ribotoxic stress response (RSR). The Shiga toxin-induced RSR is known to involve the activation of the stress-activated protein kinases (SAPKs) p38 and JNK. In some cell types, Stx also can induce the classical mitogen-activated protein kinases (MAPKs) or ERK1/2, but the mechanism(s) by which this activation occurs is unknown. In this study, we investigated the mechanism by which Stx activates ERK1/2s in IECs and the contribution of ERK1/2 activation to interleukin-8 (IL-8) expression. We demonstrate that Stx1 activates ERK1/2 in a biphasic manner: the first phase occurs in response to StxB1 subunit, while the second phase requires StxA1 subunit activity. We show that the A subunit-dependent ERK1/2 activation is mediated through ZAK-dependent signaling, and inhibition of ERK1/2 activation via the MEK1/2 inhibitors U0126 and PD98059 results in decreased Stx1-mediated IL-8 mRNA. Finally, we demonstrate that ERK1/2 are activatedin vivoin the colon of Stx2-intoxicated infant rabbits, a model in which Stx2 induces a primarily neutrophilic inflammatory response. Together, our data support a role for ERK1/2 activation in the development of Stx-mediated intestinal inflammation.

scholarly journals A Novel Zak Knockout Mouse with a Defective Ribotoxic Stress Response

Toxins ◽  
2016 ◽  
Vol 8 (9) ◽  
pp. 259 ◽  
Author(s):  
Dakshina Jandhyala ◽  
John Wong ◽  
Nicholas Mantis ◽  
Bruce Magun ◽  
John Leong ◽  
...  
Keyword(s):  
Stress Response ◽  
Knockout Mouse ◽  
Ribotoxic Stress Response

scholarly journals Serine 58 of 14-3-3ζ Is a Molecular Switch Regulating ASK1 and Oxidant Stress-Induced Cell Death

2009 ◽  
Vol 29 (15) ◽  
pp. 4167-4176 ◽  
Author(s):  
Jibin Zhou ◽  
Zhili Shao ◽  
Risto Kerkela ◽  
Hidenori Ichijo ◽  
Anthony J. Muslin ◽  
...  
Keyword(s):  
Cell Death ◽  
Stress Response ◽  
Family Member ◽  
Protein Kinases ◽  
Oxidant Stress ◽  
Critical Factor ◽  
Cell Types ◽  
Oxidant Injury ◽  
Multiple Cell ◽  
Negative Impacts

ABSTRACT Oxidant stress is a ubiquitous stressor with negative impacts on multiple cell types. ASK1 is a central mediator of oxidant injury, but while mechanisms of its inhibition, such as sequestration by 14-3-3 proteins and thioredoxin, have been identified, mechanisms of activation have remained obscure and the signaling pathways regulating this are not clear. Here, we report that phosphorylation of 14-3-3ζ at serine 58 (S58) is dynamically regulated in the cell and that the phosphorylation status of S58 is a critical factor regulating oxidant stress-induced cell death. Phosphorylation of S58 releases ASK1 from 14-3-3ζ, and ASK1 then activates stress-activated protein kinases, leading to cell death. While several members of the mammalian sterile 20 (Mst) family of kinases can phosphorylate S58 when overexpressed, we identify Ste20/oxidant stress response kinase 1 (SOK-1), an Mst family member known to be activated by oxidant stress, as a central endogenous regulator of S58 phosphorylation and thereby of ASK1-mediated cell death. Our findings identify a novel pathway that regulates ASK1 activation and oxidant stress-induced cell death.

The role of receptor-like protein kinases (RLKs) in abiotic stress response in plants

2016 ◽  
Vol 36 (2) ◽  
pp. 235-242 ◽  
Author(s):  
Yaoyao Ye ◽  
Yanfei Ding ◽  
Qiong Jiang ◽  
Feijuan Wang ◽  
Junwei Sun ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Stress Response ◽  
Protein Kinases ◽  
Abiotic Stress Response
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