Regulation of ROS signal transduction by NADPH oxidase 4 localization

Reactive oxygen species (ROS) function as intracellular signaling molecules in a diverse range of biological processes. However, it is unclear how freely diffusible ROS dictate specific cellular responses. In this study, we demonstrate that nicotinamide adenine dinucleotide phosphate reduced oxidase...

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Vydáno v:	The Journal of cell biology Ročník 181; číslo 7; s. 1129
Hlavní autoři:	Chen, Kai, Kirber, Michael T, Xiao, Hui, Yang, Yu, Keaney, Jr, John F
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 30.06.2008
Témata:	Animals Antioxidants - pharmacology Cell Proliferation - drug effects Chlorocebus aethiops COS Cells Endoplasmic Reticulum - drug effects Endoplasmic Reticulum - enzymology Endothelial Cells - cytology Endothelial Cells - drug effects Endothelial Cells - enzymology Epidermal Growth Factor - pharmacology ErbB Receptors - metabolism Humans Mice Mutation - genetics NADPH Oxidase 4 NADPH Oxidases - metabolism Oxidation-Reduction - drug effects Phosphorylation - drug effects Protein Transport - drug effects Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism Reactive Oxygen Species - metabolism Signal Transduction - drug effects Substrate Specificity - drug effects
ISSN:	1540-8140, 1540-8140
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Abstract	Reactive oxygen species (ROS) function as intracellular signaling molecules in a diverse range of biological processes. However, it is unclear how freely diffusible ROS dictate specific cellular responses. In this study, we demonstrate that nicotinamide adenine dinucleotide phosphate reduced oxidase 4 (Nox4), a major Nox isoform expressed in nonphagocytic cells, including vascular endothelium, is localized to the endoplasmic reticulum (ER). ER localization of Nox4 is critical for the regulation of protein tyrosine phosphatase (PTP) 1B, also an ER resident, through redox-mediated signaling. Nox4-mediated oxidation and inactivation of PTP1B in the ER serves as a regulatory switch for epidermal growth factor (EGF) receptor trafficking and specifically acts to terminate EGF signaling. Consistent with this notion, PTP1B oxidation could also be modulated by ER targeting of antioxidant enzymes but not their untargeted counterparts. These data indicate that the specificity of intracellular ROS-mediated signal transduction may be modulated by the localization of Nox isoforms within specific subcellular compartments.
AbstractList	Reactive oxygen species (ROS) function as intracellular signaling molecules in a diverse range of biological processes. However, it is unclear how freely diffusible ROS dictate specific cellular responses. In this study, we demonstrate that nicotinamide adenine dinucleotide phosphate reduced oxidase 4 (Nox4), a major Nox isoform expressed in nonphagocytic cells, including vascular endothelium, is localized to the endoplasmic reticulum (ER). ER localization of Nox4 is critical for the regulation of protein tyrosine phosphatase (PTP) 1B, also an ER resident, through redox-mediated signaling. Nox4-mediated oxidation and inactivation of PTP1B in the ER serves as a regulatory switch for epidermal growth factor (EGF) receptor trafficking and specifically acts to terminate EGF signaling. Consistent with this notion, PTP1B oxidation could also be modulated by ER targeting of antioxidant enzymes but not their untargeted counterparts. These data indicate that the specificity of intracellular ROS-mediated signal transduction may be modulated by the localization of Nox isoforms within specific subcellular compartments.Reactive oxygen species (ROS) function as intracellular signaling molecules in a diverse range of biological processes. However, it is unclear how freely diffusible ROS dictate specific cellular responses. In this study, we demonstrate that nicotinamide adenine dinucleotide phosphate reduced oxidase 4 (Nox4), a major Nox isoform expressed in nonphagocytic cells, including vascular endothelium, is localized to the endoplasmic reticulum (ER). ER localization of Nox4 is critical for the regulation of protein tyrosine phosphatase (PTP) 1B, also an ER resident, through redox-mediated signaling. Nox4-mediated oxidation and inactivation of PTP1B in the ER serves as a regulatory switch for epidermal growth factor (EGF) receptor trafficking and specifically acts to terminate EGF signaling. Consistent with this notion, PTP1B oxidation could also be modulated by ER targeting of antioxidant enzymes but not their untargeted counterparts. These data indicate that the specificity of intracellular ROS-mediated signal transduction may be modulated by the localization of Nox isoforms within specific subcellular compartments. Reactive oxygen species (ROS) function as intracellular signaling molecules in a diverse range of biological processes. However, it is unclear how freely diffusible ROS dictate specific cellular responses. In this study, we demonstrate that nicotinamide adenine dinucleotide phosphate reduced oxidase 4 (Nox4), a major Nox isoform expressed in nonphagocytic cells, including vascular endothelium, is localized to the endoplasmic reticulum (ER). ER localization of Nox4 is critical for the regulation of protein tyrosine phosphatase (PTP) 1B, also an ER resident, through redox-mediated signaling. Nox4-mediated oxidation and inactivation of PTP1B in the ER serves as a regulatory switch for epidermal growth factor (EGF) receptor trafficking and specifically acts to terminate EGF signaling. Consistent with this notion, PTP1B oxidation could also be modulated by ER targeting of antioxidant enzymes but not their untargeted counterparts. These data indicate that the specificity of intracellular ROS-mediated signal transduction may be modulated by the localization of Nox isoforms within specific subcellular compartments.
Author	Chen, Kai Keaney, Jr, John F Kirber, Michael T Xiao, Hui Yang, Yu
Author_xml	– sequence: 1 givenname: Kai surname: Chen fullname: Chen, Kai email: kai.chen@umassmed.edu organization: Department of Medicine, Division of Cardiovascular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA. kai.chen@umassmed.edu – sequence: 2 givenname: Michael T surname: Kirber fullname: Kirber, Michael T – sequence: 3 givenname: Hui surname: Xiao fullname: Xiao, Hui – sequence: 4 givenname: Yu surname: Yang fullname: Yang, Yu – sequence: 5 givenname: John F surname: Keaney, Jr fullname: Keaney, Jr, John F
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/18573911$$D View this record in MEDLINE/PubMed
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PublicationTitle	The Journal of cell biology
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Snippet	Reactive oxygen species (ROS) function as intracellular signaling molecules in a diverse range of biological processes. However, it is unclear how freely...
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SubjectTerms	Animals Antioxidants - pharmacology Cell Proliferation - drug effects Chlorocebus aethiops COS Cells Endoplasmic Reticulum - drug effects Endoplasmic Reticulum - enzymology Endothelial Cells - cytology Endothelial Cells - drug effects Endothelial Cells - enzymology Epidermal Growth Factor - pharmacology ErbB Receptors - metabolism Humans Mice Mutation - genetics NADPH Oxidase 4 NADPH Oxidases - metabolism Oxidation-Reduction - drug effects Phosphorylation - drug effects Protein Transport - drug effects Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism Reactive Oxygen Species - metabolism Signal Transduction - drug effects Substrate Specificity - drug effects
Title	Regulation of ROS signal transduction by NADPH oxidase 4 localization
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