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      Adapting the Stress Response: Viral Subversion of the mTOR Signaling Pathway

      review-article
      Author(s): 1 , 1 , 2 , 1 , 2 , 1 , 2 , *
      Editor(s):
      Publication date (Electronic):
      Journal: Viruses
      Publisher: MDPI
      Keywords: PI3K, Akt, mTOR, virus, 4EBP1, autophagy

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          Abstract

          The mammalian target of rapamycin (mTOR) is a central regulator of gene expression, translation and various metabolic processes. Multiple extracellular (growth factors) and intracellular (energy status) molecular signals as well as a variety of stressors are integrated into the mTOR pathway. Viral infection is a significant stress that can activate, reduce or even suppress the mTOR signaling pathway. Consequently, viruses have evolved a plethora of different mechanisms to attack and co-opt the mTOR pathway in order to make the host cell a hospitable environment for replication. A more comprehensive knowledge of different viral interactions may provide fruitful targets for new antiviral drugs.

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          Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis.

          Megan Cully, Han You, Arnold J. Levine … (2006)
          The tumour-suppressor phosphatase with tensin homology (PTEN) is the most important negative regulator of the cell-survival signalling pathway initiated by phosphatidylinositol 3-kinase (PI3K). Although PTEN is mutated or deleted in many tumours, deregulation of the PI3K-PTEN network also occurs through other mechanisms. Crosstalk between the PI3K pathways and other tumorigenic signalling pathways, such as those that involve Ras, p53, TOR (target of rapamycin) or DJ1, can contribute to this deregulation. How does the PI3K pathway integrate signals from numerous sources, and how can this information be used in the rational design of cancer therapies?
          Article 0 comments Cited 282 times – based on 0 reviews     Review now
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            Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes.

            Monique Gannagé, Dorothee Dormann, Randy A. Albrecht … (2009)
            Influenza A virus is an important human pathogen causing significant morbidity and mortality every year and threatening the human population with epidemics and pandemics. Therefore, it is important to understand the biology of this virus to develop strategies to control its pathogenicity. Here, we demonstrate that influenza A virus inhibits macroautophagy, a cellular process known to be manipulated by diverse pathogens. Influenza A virus infection causes accumulation of autophagosomes by blocking their fusion with lysosomes, and one viral protein, matrix protein 2, is necessary and sufficient for this inhibition of autophagosome degradation. Macroautophagy inhibition by matrix protein 2 compromises survival of influenza virus-infected cells but does not influence viral replication. We propose that influenza A virus, which also encodes proapoptotic proteins, is able to determine the death of its host cell by inducing apoptosis and also by blocking macroautophagy.
            Article 0 comments Cited 212 times – based on 0 reviews     Review now
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              A complex interplay between Akt, TSC2 and the two mTOR complexes.

              Jingxiang Huang, Brendan D Manning (2009)
              Akt/PKB (protein kinase B) both regulates and is regulated by the TSC (tuberous sclerosis complex) 1-TSC2 complex. Downstream of PI3K (phosphoinositide 3-kinase), Akt phosphorylates TSC2 directly on multiple sites. Although the molecular mechanism is not well understood, these phosphorylation events relieve the inhibitory effects of the TSC1-TSC2 complex on Rheb and mTORC1 [mTOR (mammalian target of rapamycin) complex] 1, thereby activating mTORC1 in response to growth factors. Through negative-feedback mechanisms, mTORC1 activity inhibits growth factor stimulation of PI3K. This is particularly evident in cells and tumours lacking the TSC1-TSC2 complex, where Akt signalling is severely attenuated due, at least in part, to constitutive activation of mTORC1. An additional level of complexity in the relationship between Akt and the TSC1-TSC2 complex has recently been uncovered. The growth-factor-stimulated kinase activity of mTORC2 [also known as the mTOR-rictor (rapamycin-insensitive companion of mTOR) complex], which normally enhances Akt signalling by phosphorylating its hydrophobic motif (Ser(473)), was found to be defective in cells lacking the TSC1-TSC2 complex. This effect on mTORC2 can be separated from the inhibitory effects of the TSC1-TSC2 complex on Rheb and mTORC1. The present review discusses our current understanding of the increasingly complex functional interactions between Akt, the TSC1-TSC2 complex and mTOR, which are fundamentally important players in a large variety of human diseases.
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                Author and article information

                Contributors
                Craig McCormick: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Viruses
                Journal ID (iso-abbrev): Viruses
                Journal ID (publisher-id): viruses
                Title: Viruses
                Publisher: MDPI
                ISSN (Electronic): 1999-4915
                Publication date (Electronic): 24 May 2016
                Publication date Collection: June 2016
                Volume: 8
                Issue: 6
                Electronic Location Identifier: 152
                Affiliations
                [1 ]HIV-1 RNA Trafficking Laboratory, Lady Davis Institute at the Jewish General Hospital, Montréal, QC H3T 1E2, Canada; vle_sage@ 123456hotmail.com (V.L.S.); alessandro.cinti@ 123456mail.mcgill.ca (A.C.); raquel.amorim@ 123456mail.mcgill.ca (R.A.)
                [2 ]Department of Medicine, McGill University, Montréal, QC H3A 0G4, Canada
                Author notes
                [* ]Correspondence: andrew.mouland@ 123456mcgill.ca ; Tel.: +1-514-340-8260
                Article
                Publisher ID: viruses-08-00152
                DOI: 10.3390/v8060152
                PMC ID: 4926172
                PubMed ID: 27231932
                SO-VID: 2be799bc-ae20-4461-9e00-3be56b18c669
                Copyright © © 2016 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 28 April 2016
                Date accepted : 19 May 2016
                Categories
                Subject: Review

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: pi3k,akt,mtor,virus,4ebp1,autophagy
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: pi3k, akt, mtor, virus, 4ebp1, autophagy

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