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The Endoplasmic Reticulum Chaperone Calnexin Is a NADPH Oxidase NOX4 Interacting Protein

Prior, Kim-Kristin ; Wittig, Ilka ; Leisegang, Matthias S. ; Groenendyk, Jody ; Weissmann, Norbert ; Michalak, Marek ; Jansen-Dürr, Pidder ; Shah, Ajay M. ; Brandes, Ralf P.

The Journal of biological chemistry, 2016-03, Vol.291 (13), p.7045-7059 [Periódico revisado por pares]

United States: Elsevier Inc

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Título:
The Endoplasmic Reticulum Chaperone Calnexin Is a NADPH Oxidase NOX4 Interacting Protein
Autor: Prior, Kim-Kristin ; Wittig, Ilka ; Leisegang, Matthias S. ; Groenendyk, Jody ; Weissmann, Norbert ; Michalak, Marek ; Jansen-Dürr, Pidder ; Shah, Ajay M. ; Brandes, Ralf P.
Assuntos: Animals ; blue native PAGE ; Calnexin - antagonists & inhibitors ; Calnexin - genetics ; Calnexin - metabolism ; Cell Biology ; Cell Line ; Endoplasmic Reticulum - chemistry ; Endoplasmic Reticulum - metabolism ; Fibroblasts - cytology ; Fibroblasts - metabolism ; Gene Expression ; HEK293 Cells ; Humans ; Immunoprecipitation ; Isotope Labeling ; mass spectrometry (MS) ; Mice ; Mice, Knockout ; NADPH oxidase ; NADPH Oxidase 4 ; NADPH Oxidases - genetics ; NADPH Oxidases - metabolism ; Protein Binding ; protein-protein interaction ; proteomics ; reactive oxygen species (ROS) ; Reactive Oxygen Species - metabolism ; RNA, Small Interfering - genetics ; RNA, Small Interfering - metabolism
É parte de: The Journal of biological chemistry, 2016-03, Vol.291 (13), p.7045-7059
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Supported by the Austrian Research Promotion Agency (FFG) Grant 848474.
Supported by the British Heart Foundation.
Descrição: Within the family of NADPH oxidases, NOX4 is unique as it is predominantly localized in the endoplasmic reticulum, has constitutive activity, and generates hydrogen peroxide (H2O2). We hypothesize that these features are consequences of a so far unidentified NOX4-interacting protein. Two-dimensional blue native (BN) electrophorese combined with SDS-PAGE yielded NOX4 to reside in macromolecular complexes. Interacting proteins were screened by quantitative SILAC (stable isotope labeling of amino acids in cell culture) co-immunoprecipitation (Co-IP) in HEK293 cells stably overexpressing NOX4. By this technique, several interacting proteins were identified with calnexin showing the most robust interaction. Calnexin also resided in NOX4-containing complexes as demonstrated by complexome profiling from BN-PAGE. The calnexin NOX4 interaction could be confirmed by reverse Co-IP and proximity ligation assay, whereas NOX1, NOX2, or NOX5 did not interact with calnexin. Calnexin deficiency as studied in mouse embryonic fibroblasts from calnexin−/− mice or in response to calnexin shRNA reduced cellular NOX4 protein expression and reactive oxygen species formation. Our results suggest that endogenous NOX4 forms macromolecular complexes with calnexin, which are needed for the proper maturation, processing, and function of NOX4 in the endoplasmic reticulum.
Editor: United States: Elsevier Inc
Idioma: Inglês

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The Endoplasmic Reticulum Chaperone Calnexin Is a NADPH Oxidase NOX4 Interacting Protein

Prior, Kim-Kristin ; Wittig, Ilka ; Leisegang, Matthias S. ; Groenendyk, Jody ; Weissmann, Norbert ; Michalak, Marek ; Jansen-Dürr, Pidder ; Shah, Ajay M. ; Brandes, Ralf P.

United States: Elsevier Inc

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