Histone deacetylase isoforms regulate innate immune responses by deacetylating mitogen-activated protein kinase phosphatase-1

2013 ◽  
Vol 95 (4) ◽  
pp. 651-659 ◽  
Author(s):  
Y. Jeong ◽  
R. Du ◽  
X. Zhu ◽  
S. Yin ◽  
J. Wang ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Immune Responses ◽  
Histone Deacetylase ◽  
Innate Immune ◽  
Mitogen Activated Protein Kinase ◽  
Innate Immune Responses ◽  
Mitogen Activated Protein

scholarly journals Mitogen-Activated Protein Kinase-Activated Kinase RSK2 Plays a Role in Innate Immune Responses to Influenza Virus Infection

2009 ◽  
Vol 83 (6) ◽  
pp. 2510-2517 ◽  
Author(s):  
Satoshi Kakugawa ◽  
Masayuki Shimojima ◽  
Hideo Goto ◽  
Taisuke Horimoto ◽  
Naoki Oshimori ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Protein Kinase ◽  
Virus Infection ◽  
Immune Responses ◽  
Influenza Virus Infection ◽  
Innate Immune ◽  
Mitogen Activated Protein Kinase ◽  
Innate Immune Responses ◽  
Mitogen Activated Protein ◽  
Cellular Antiviral Response

ABSTRACT Viral infections induce signaling pathways in mammalian cells that stimulate innate immune responses and affect cellular processes, such as apoptosis, mitosis, and differentiation. Here, we report that the ribosomal protein S6 kinase alpha 3 (RSK2), which is activated through the “classical” mitogen-activated protein kinase pathway, plays a role in innate immune responses to influenza virus infection. RSK2 functions in the regulation of cell growth and differentiation but was not known to play a role in the cellular antiviral response. We have found that knockdown of RSK2 enhanced viral polymerase activity and growth of influenza viruses. Influenza virus infection stimulates NK-κB- and beta interferon-dependent promoters. This stimulation was reduced in RSK2 knockdown cells, suggesting that RSK2 executes its effect through innate immune response pathways. Furthermore, RSK2 knockdown suppressed influenza virus-induced phosphorylation of the double-stranded RNA-activated protein kinase PKR, a known antiviral protein. These findings establish a role for RSK2 in the cellular antiviral response.

Dual-specificity phosphatase 1: a critical regulator of innate immune responses

2006 ◽  
Vol 34 (6) ◽  
pp. 1018-1023 ◽  
Author(s):  
S.M. Abraham ◽  
A.R. Clark
Keyword(s):  
Innate Immunity ◽  
Immune Responses ◽  
P38 Mapk ◽  
Time Course ◽  
Inflammatory Diseases ◽  
Innate Immune ◽  
Mitogen Activated Protein Kinase ◽  
Innate Immune Responses ◽  
Inflammatory Stimuli ◽  
Mitogen Activated Protein

Innate immune responses are critically dependent on MAPK (mitogen-activated protein kinase) signalling pathways, in particular JNK (c-Jun N-terminal kinase) and p38 MAPK. Both of these kinases are negatively regulated via their dephosphorylation by DUSP1 (dual­-specificity phosphatase 1). Several pro- and anti-inflammatory stimuli converge to regulate the DUSP1 gene and to modulate the time course of its expression. In turn, the pattern of expression of DUSP1 dictates the kinetics of activation of JNK and p38 MAPK, and this influences the expression of several mediators of innate immunity. DUSP1 is therefore a central regulator of innate immunity, and its expression can profoundly affect the outcome of inflammatory challenges. We discuss possible implications for immune-mediated inflammatory diseases and their treatment.

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