EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.

Mitogen Activated Protein Kinases (MAPKs) are a class of serine/threonine kinases that regulate a number of different cellular activities including cell proliferation, differentiation, survival and even death. The pathogen Entamoeba histolytica possess a single homologue of a typical MAPK gene (EhMA...

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Main Authors: Anupama Sardar Ghosh, Doel Ray, Suman Dutta, Sanghamitra Raha
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2010-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2951911?pdf=render
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spelling doaj-c06bfd20562c4cbbb56752adeaf718f22020-11-25T01:45:56ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-01-01510e1329110.1371/journal.pone.0013291EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.Anupama Sardar GhoshDoel RaySuman DuttaSanghamitra RahaMitogen Activated Protein Kinases (MAPKs) are a class of serine/threonine kinases that regulate a number of different cellular activities including cell proliferation, differentiation, survival and even death. The pathogen Entamoeba histolytica possess a single homologue of a typical MAPK gene (EhMAPK) whose identification was previously reported by us but its functional implications remained unexplored. EhMAPK, the only mitogen-activated protein kinase from the parasitic protist Entamoeba histolytica with Threonine-X-Tyrosine (TXY) phosphorylation motif was cloned, expressed in E. coli and functionally characterized under different stress conditions. The expression profile of EhMAPK at the protein and mRNA level remained similar among untreated, heat shocked and hydrogen peroxide-treated samples in all cases of dose and time. But a significant difference was obtained in the phosphorylation status of the protein in response to different stresses. Heat shock at 43°C or 0.5 mM H(2)O(2) treatment enhanced the phosphorylation status of EhMAPK and augmented the kinase activity of the protein whereas 2.0 mM H(2)O(2) treatment induced dephosphorylation of EhMAPK and loss of kinase activity. 2.0 mM H(2)O(2) treatment reduced parasite viability significantly but heat shock and 0.5 mM H(2)O(2) treatment failed to adversely affect E. histolytica viability. Therefore, a distinct possibility that activation of EhMAPK is associated with stress survival in E. histolytica is seen. Our study also gives a glimpse of the regulatory mechanism of the protein under in vivo conditions. Since the parasite genome lacks any typical homologue of mammalian MEK, the dual specificity kinases which are the upstream activators of MAPK, indications of the existence of some alternate regulatory mechanisms of the EhMAPK activity is perceived. These may include the autophosphorylation activity of the protein itself in combination with some upstream phosphatases which are not yet identified.http://europepmc.org/articles/PMC2951911?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Anupama Sardar Ghosh
Doel Ray
Suman Dutta
Sanghamitra Raha
spellingShingle Anupama Sardar Ghosh
Doel Ray
Suman Dutta
Sanghamitra Raha
EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.
PLoS ONE
author_facet Anupama Sardar Ghosh
Doel Ray
Suman Dutta
Sanghamitra Raha
author_sort Anupama Sardar Ghosh
title EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.
title_short EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.
title_full EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.
title_fullStr EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.
title_full_unstemmed EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival.
title_sort ehmapk, the mitogen-activated protein kinase from entamoeba histolytica is associated with cell survival.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2010-01-01
description Mitogen Activated Protein Kinases (MAPKs) are a class of serine/threonine kinases that regulate a number of different cellular activities including cell proliferation, differentiation, survival and even death. The pathogen Entamoeba histolytica possess a single homologue of a typical MAPK gene (EhMAPK) whose identification was previously reported by us but its functional implications remained unexplored. EhMAPK, the only mitogen-activated protein kinase from the parasitic protist Entamoeba histolytica with Threonine-X-Tyrosine (TXY) phosphorylation motif was cloned, expressed in E. coli and functionally characterized under different stress conditions. The expression profile of EhMAPK at the protein and mRNA level remained similar among untreated, heat shocked and hydrogen peroxide-treated samples in all cases of dose and time. But a significant difference was obtained in the phosphorylation status of the protein in response to different stresses. Heat shock at 43°C or 0.5 mM H(2)O(2) treatment enhanced the phosphorylation status of EhMAPK and augmented the kinase activity of the protein whereas 2.0 mM H(2)O(2) treatment induced dephosphorylation of EhMAPK and loss of kinase activity. 2.0 mM H(2)O(2) treatment reduced parasite viability significantly but heat shock and 0.5 mM H(2)O(2) treatment failed to adversely affect E. histolytica viability. Therefore, a distinct possibility that activation of EhMAPK is associated with stress survival in E. histolytica is seen. Our study also gives a glimpse of the regulatory mechanism of the protein under in vivo conditions. Since the parasite genome lacks any typical homologue of mammalian MEK, the dual specificity kinases which are the upstream activators of MAPK, indications of the existence of some alternate regulatory mechanisms of the EhMAPK activity is perceived. These may include the autophosphorylation activity of the protein itself in combination with some upstream phosphatases which are not yet identified.
url http://europepmc.org/articles/PMC2951911?pdf=render
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