Robustness and dissipation of mitogen-activated protein kinases signal transduction network: Underlying funneled landscape against stochastic fluctuations

2008 ◽  
Vol 129 (13) ◽  
pp. 135101 ◽  
Author(s):  
Jin Wang ◽  
Kun Zhang ◽  
Erkwang Wang
Keyword(s):  
Signal Transduction ◽  
Protein Kinases ◽  
Signal Transduction Network ◽  
Mitogen Activated Protein Kinases ◽  
Stochastic Fluctuations ◽  
Mitogen Activated Protein

scholarly journals Mitogen-Activated Protein Kinases: Functions in Signal Transduction and Human Diseases

2019 ◽  
Vol 20 (19) ◽  
pp. 4844 ◽  
Author(s):  
Ritva Tikkanen ◽  
David J. Nikolic-Paterson
Keyword(s):  
Signal Transduction ◽  
Growth Factors ◽  
Protein Kinases ◽  
Human Diseases ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

Mitogen-activated protein kinases (MAPKs) are involved in signaling processes induced by various stimuli, such as growth factors, stress, or even autoantibodies [...]

scholarly journals Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability

2019 ◽  
Vol 20 (11) ◽  
pp. 2668 ◽  
Author(s):  
Hsueh-Fen Chen ◽  
Huai-Chia Chuang ◽  
Tse-Hua Tan
Keyword(s):  
Signal Transduction ◽  
Protein Stability ◽  
Protein Kinases ◽  
Post Translational Modifications ◽  
Mitogen Activated Protein Kinases ◽  
Cell Responses ◽  
Dual Specificity ◽  
Duration Magnitude ◽  
Mitogen Activated Protein ◽  
Dual Specificity Phosphatases

Mitogen-activated protein kinases (MAPKs) are key regulators of signal transduction and cell responses. Abnormalities in MAPKs are associated with multiple diseases. Dual-specificity phosphatases (DUSPs) dephosphorylate many key signaling molecules, including MAPKs, leading to the regulation of duration, magnitude, or spatiotemporal profiles of MAPK activities. Hence, DUSPs need to be properly controlled. Protein post-translational modifications, such as ubiquitination, phosphorylation, methylation, and acetylation, play important roles in the regulation of protein stability and activity. Ubiquitination is critical for controlling protein degradation, activation, and interaction. For DUSPs, ubiquitination induces degradation of eight DUSPs, namely, DUSP1, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, and DUSP16. In addition, protein stability of DUSP2 and DUSP10 is enhanced by phosphorylation. Methylation-induced ubiquitination of DUSP14 stimulates its phosphatase activity. In this review, we summarize the knowledge of the regulation of DUSP stability and ubiquitination through post-translational modifications.

TP5 Triggers Signal Transduction Involving Mitogen Activated Protein Kinases in Monocytes

1999 ◽  
Vol 19 (1-4) ◽  
pp. 155-166 ◽  
Author(s):  
S. Gonser ◽  
N. E. A. Crompton ◽  
P. J. A. Weber ◽  
A. G. Beck-Sickinger ◽  
G. Folkers
Keyword(s):  
Signal Transduction ◽  
Protein Kinases ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

Signal Transduction by Mitogen-activated Protein Kinases (MAPKs)

2001 ◽  
pp. 321-330
Author(s):  
Erwin Heberle-Bors ◽  
Ornella Calderini ◽  
Viktor Voronin ◽  
Cathal Wilson
Keyword(s):  
Signal Transduction ◽  
Protein Kinases ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

scholarly journals Mitogen activated protein kinases function as a cohort during a plant defense response

2018 ◽  
Author(s):  
Brant T. McNeece ◽  
Keshav Sharma ◽  
Gary W. Lawrence ◽  
Kathy S. Lawrence ◽  
Vincent P. Klink
Keyword(s):  
Gene Expression ◽  
Signal Transduction ◽  
Protein Kinases ◽  
Defense Response ◽  
Defense Genes ◽  
Root Cells ◽  
Mitogen Activated Protein Kinases ◽  
Molecular Pattern ◽  
Mitogen Activated Protein ◽  
Effector Triggered Immunity

ABSTRACTMitogen activated protein kinases (MAPKs) play important signal transduction roles. However, little is known regarding whether MAPKs influence the gene expression of other family members and the relationship that expression has to a biological process. Transcriptomic studies have identified MAPK gene expression occurring within root cells undergoing a defense response to a pathogenic event in the allotetraploidGlycine max. Furthermore, functional analyses are presented for its 32 MAPKs revealing 9 of the 32 MAPKs have a defense role, including homologs ofArabidopsis thalianaMAPK (MPK) MPK2, MPK3, MPK4, MPK5, MPK6, MPK13, MPK16 and MPK20. Defense signal transduction processes occurring through pathogen activated molecular pattern (PAMP) triggered immunity (PTI) and effector triggered immunity (ETI) have been determined in relation to these MAPKs. PTI has been analyzed by examiningBOTRYTIS INDUCED KINASE1(BIK1),ENHANCED DISEASE SUSCEPTIBILITY1(EDS1) andLESION SIMULATING DISEASE1(LSD1). ETI has been analyzed by examining the role of the bacterial effector protein harpin and the downstream cell membrane receptorNON-RACE SPECIFIC DISEASE RESISTANCE1(NDR1). Experiments have identified 5 different types of gene expression relating to MAPK expression. The MAPKs are shown to influence PTI and ETI gene expression and a panel of proven defense genes including an ABC-G type transporter, 20S membrane fusion particle components, glycoside biosynthesis, carbon metabolism, hemicellulose modification, transcription andPATHOGENESIS RELATED 1(PR1). The experiments show MAPKs broadly influence the expression of other defense MAPKs, including the co-regulation of parologous MAPKs and reveal its relationship to proven defense genes.

scholarly journals BMP7 improves insulin signal transduction in the liver via inhibition of mitogen-activated protein kinases

2019 ◽  
Vol 243 (2) ◽  
pp. 97-110 ◽  
Author(s):  
Hong Ma ◽  
Jin Yuan ◽  
Jinyu Ma ◽  
Jie Ding ◽  
Weiwei Lin ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Insulin Sensitivity ◽  
Protein Kinases ◽  
Transforming Growth Factor ◽  
Mitogen Activated Protein Kinases ◽  
Insulin Signal Transduction ◽  
Insulin Signal ◽  
Insulin Resistant ◽  
Mitogen Activated Protein

Bone morphogenetic protein 7 (BMP7), a member of the transforming growth factor-β (TGF-β) family, plays pivotal roles in energy expenditure. However, whether and how BMP7 regulates hepatic insulin sensitivity is still poorly understood. Here, we show that hepatic BMP7 expression is reduced in high-fat diet (HFD)-induced diabetic mice and palmitate (PA)-induced insulin-resistant HepG2 and AML12 cells. BMP7 improves insulin signaling pathway in insulin resistant hepatocytes. On the contrary, knockdown of BMP7 further impairs insulin signal transduction in PA-treated cells. Increased expression of BMP7 by adenovirus expressing BMP7 improves hyperglycemia, insulin sensitivity and insulin signal transduction. Furthermore, BMP7 inhibits mitogen-activated protein kinases (MAPKs) in both the liver of obese mice and PA-treated cells. In addition, inhibition of MAPKs recapitulates the effects of BMP7 on insulin signal transduction in cultured hepatocytes treated with PA. Activation of p38 MAPK abolishes the BMP7-mediated upregulation of insulin signal transduction both in vitro and in vivo. Together, our results show that hepatic BMP7 has a novel function in regulating insulin sensitivity through inhibition of MAPKs, thus providing new insights into treating insulin resistance-related disorders such as type 2 diabetes.

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