Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR

The mammalian immune system has the ability to discriminate between pathogenic and non-pathogenic microbes to control inflammation. Here we investigated ubiquitinylation profiles of host proteins after infection of macrophages with a virulent strain of the intracellular bacterium Legionella pneumoph...

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Main Authors:	Ivanov, Stanimir S., Roy, Craig R.
Format:	Online
Language:	English
Published:	2013
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3839319/

id	pubmed-3839319
recordtype	oai_dc
spelling	pubmed-38393192014-06-01 Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR Ivanov, Stanimir S. Roy, Craig R. Article The mammalian immune system has the ability to discriminate between pathogenic and non-pathogenic microbes to control inflammation. Here we investigated ubiquitinylation profiles of host proteins after infection of macrophages with a virulent strain of the intracellular bacterium Legionella pneumophila and a non-pathogenic mutant. Only infection with pathogenic Legionella resulted in ubiquitinylation of positive regulators of the metabolic checkpoint kinase mTOR leading to diminished mTOR activity. Detection of pathogen signatures resulted in translational biasing to proinflammatory cytokines through mTOR-mediated regulation of cap-dependent translation. Thus, there is a pathogen detection program in macrophages that stimulates protein ubiquitinylation and degradation of mTOR regulators, which suppresses mTOR function and directs a proinflammatory cytokine program. 2013-10-13 2013-12 /pmc/articles/PMC3839319/ /pubmed/24121838 http://dx.doi.org/10.1038/ni.2740 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Ivanov, Stanimir S. Roy, Craig R.
spellingShingle	Ivanov, Stanimir S. Roy, Craig R. Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR
author_facet	Ivanov, Stanimir S. Roy, Craig R.
author_sort	Ivanov, Stanimir S.
title	Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR
title_short	Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR
title_full	Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR
title_fullStr	Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR
title_full_unstemmed	Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR
title_sort	pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mtor
description	The mammalian immune system has the ability to discriminate between pathogenic and non-pathogenic microbes to control inflammation. Here we investigated ubiquitinylation profiles of host proteins after infection of macrophages with a virulent strain of the intracellular bacterium Legionella pneumophila and a non-pathogenic mutant. Only infection with pathogenic Legionella resulted in ubiquitinylation of positive regulators of the metabolic checkpoint kinase mTOR leading to diminished mTOR activity. Detection of pathogen signatures resulted in translational biasing to proinflammatory cytokines through mTOR-mediated regulation of cap-dependent translation. Thus, there is a pathogen detection program in macrophages that stimulates protein ubiquitinylation and degradation of mTOR regulators, which suppresses mTOR function and directs a proinflammatory cytokine program.
publishDate	2013
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3839319/
_version_	1612030328740773888

Pathogen signatures activate a ubiquitinylation pathway that modulates function of the metabolic checkpoint kinase mTOR

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