Dual-Specificity Phosphatase 1 and Tristetraprolin Cooperate To Regulate Macrophage Responses to Lipopolysaccharide
Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It functions as an essential negative regulator of innate immune responses, hence disruption of the Dusp1 gene renders mice extremely sensitive to a wide...
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| Published in | The Journal of immunology (1950) Vol. 195; no. 1; pp. 277 - 288 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
AAI
01.07.2015
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| Abstract | Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It functions as an essential negative regulator of innate immune responses, hence disruption of the Dusp1 gene renders mice extremely sensitive to a wide variety of experimental inflammatory challenges. The principal mechanisms behind the overexpression of inflammatory mediators by Dusp1(-/-) cells are not known. In this study, we use a genetic approach to identify an important mechanism of action of DUSP1, involving the modulation of the activity of the mRNA-destabilizing protein tristetraprolin. This mechanism is key to the control of essential early mediators of inflammation, TNF, CXCL1, and CXCL2, as well as the anti-inflammatory cytokine IL-10. The same mechanism also contributes to the regulation of a large number of transcripts induced by treatment of macrophages with LPS. These findings demonstrate that modulation of the phosphorylation status of tristetraprolin is an important physiological mechanism by which innate immune responses can be controlled. |
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| AbstractList | Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38 alpha , and p38 beta MAPKs. It functions as an essential negative regulator of innate immune responses, hence disruption of the Dusp1 gene renders mice extremely sensitive to a wide variety of experimental inflammatory challenges. The principal mechanisms behind the overexpression of inflammatory mediators by Dusp1-/- cells are not known. In this study, we use a genetic approach to identify an important mechanism of action of DUSP1, involving the modulation of the activity of the mRNA-destabilizing protein tristetraprolin. This mechanism is key to the control of essential early mediators of inflammation, TNF, CXCL1, and CXCL2, as well as the anti-inflammatory cytokine IL-10. The same mechanism also contributes to the regulation of a large number of transcripts induced by treatment of macrophages with LPS. These findings demonstrate that modulation of the phosphorylation status of tristetraprolin is an important physiological mechanism by which innate immune responses can be controlled. Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It functions as an essential negative regulator of innate immune responses, hence disruption of the Dusp1 gene renders mice extremely sensitive to a wide variety of experimental inflammatory challenges. The principal mechanisms behind the overexpression of inflammatory mediators by Dusp1(-/-) cells are not known. In this study, we use a genetic approach to identify an important mechanism of action of DUSP1, involving the modulation of the activity of the mRNA-destabilizing protein tristetraprolin. This mechanism is key to the control of essential early mediators of inflammation, TNF, CXCL1, and CXCL2, as well as the anti-inflammatory cytokine IL-10. The same mechanism also contributes to the regulation of a large number of transcripts induced by treatment of macrophages with LPS. These findings demonstrate that modulation of the phosphorylation status of tristetraprolin is an important physiological mechanism by which innate immune responses can be controlled. Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It functions as an essential negative regulator of innate immune responses, hence disruption of the Dusp1 gene renders mice extremely sensitive to a wide variety of experimental inflammatory challenges. The principal mechanisms behind the overexpression of inflammatory mediators by Dusp1 −/− cells are not known. In this study, we use a genetic approach to identify an important mechanism of action of DUSP1, involving the modulation of the activity of the mRNA-destabilizing protein tristetraprolin. This mechanism is key to the control of essential early mediators of inflammation, TNF, CXCL1, and CXCL2, as well as the anti-inflammatory cytokine IL-10. The same mechanism also contributes to the regulation of a large number of transcripts induced by treatment of macrophages with LPS. These findings demonstrate that modulation of the phosphorylation status of tristetraprolin is an important physiological mechanism by which innate immune responses can be controlled. Abstract Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It functions as an essential negative regulator of innate immune responses, hence disruption of the Dusp1 gene renders mice extremely sensitive to a wide variety of experimental inflammatory challenges. The principal mechanisms behind the overexpression of inflammatory mediators by Dusp1−/− cells are not known. In this study, we use a genetic approach to identify an important mechanism of action of DUSP1, involving the modulation of the activity of the mRNA-destabilizing protein tristetraprolin. This mechanism is key to the control of essential early mediators of inflammation, TNF, CXCL1, and CXCL2, as well as the anti-inflammatory cytokine IL-10. The same mechanism also contributes to the regulation of a large number of transcripts induced by treatment of macrophages with LPS. These findings demonstrate that modulation of the phosphorylation status of tristetraprolin is an important physiological mechanism by which innate immune responses can be controlled. |
| Author | Ross, Ewan A Rosner, Dalya R Clark, Andrew R Saklatvala, Jeremy Dean, Jonathan L Cunliffe, Helen E Ammit, Alaina J Tang, Tina Smallie, Tim Ridley, Michael L Buckley, Christopher D |
| Author_xml | – sequence: 1 givenname: Tim surname: Smallie fullname: Smallie, Tim organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 2 givenname: Ewan A surname: Ross fullname: Ross, Ewan A organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 3 givenname: Alaina J surname: Ammit fullname: Ammit, Alaina J organization: Faculty of Pharmacy, The University of Sydney, New South Wales 2006, Australia; and – sequence: 4 givenname: Helen E surname: Cunliffe fullname: Cunliffe, Helen E organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 5 givenname: Tina surname: Tang fullname: Tang, Tina organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 6 givenname: Dalya R surname: Rosner fullname: Rosner, Dalya R organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 7 givenname: Michael L surname: Ridley fullname: Ridley, Michael L organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 8 givenname: Christopher D surname: Buckley fullname: Buckley, Christopher D organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom – sequence: 9 givenname: Jeremy surname: Saklatvala fullname: Saklatvala, Jeremy organization: Kennedy Institute of Rheumatology, Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, University of Oxford, Oxford OX3 7FY, United Kingdom – sequence: 10 givenname: Jonathan L surname: Dean fullname: Dean, Jonathan L organization: Kennedy Institute of Rheumatology, Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, University of Oxford, Oxford OX3 7FY, United Kingdom – sequence: 11 givenname: Andrew R surname: Clark fullname: Clark, Andrew R email: a.r.clark@bham.ac.uk organization: School of Immunity and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, United Kingdom; a.r.clark@bham.ac.uk |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26019272$$D View this record in MEDLINE/PubMed |
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| Snippet | Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It functions... Abstract Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38α, and p38β MAPKs. It... Dual-specificity phosphatase (DUSP) 1 dephosphorylates and inactivates members of the MAPK superfamily, in particular, JNKs, p38 alpha , and p38 beta MAPKs. It... |
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| SubjectTerms | Animals Chemokine CXCL1 - genetics Chemokine CXCL1 - immunology Chemokine CXCL2 - genetics Chemokine CXCL2 - immunology Dual Specificity Phosphatase 1 - genetics Dual Specificity Phosphatase 1 - immunology Gene Expression Regulation Immunity, Innate Innate Immunity and Inflammation Interleukin-10 - genetics Interleukin-10 - immunology Lipopolysaccharides - pharmacology Macrophages - drug effects Macrophages - immunology Macrophages - pathology MAP Kinase Kinase 4 - genetics MAP Kinase Kinase 4 - immunology Mice Mice, Inbred C57BL Mitogen-Activated Protein Kinase 11 - genetics Mitogen-Activated Protein Kinase 11 - immunology Mitogen-Activated Protein Kinase 14 - genetics Mitogen-Activated Protein Kinase 14 - immunology Phosphorylation Primary Cell Culture RNA Stability RNA, Messenger - genetics RNA, Messenger - immunology Signal Transduction Tristetraprolin - genetics Tristetraprolin - immunology Tumor Necrosis Factor-alpha - genetics Tumor Necrosis Factor-alpha - immunology |
| Title | Dual-Specificity Phosphatase 1 and Tristetraprolin Cooperate To Regulate Macrophage Responses to Lipopolysaccharide |
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