Within the family of NADPH oxidases, Nox4 is unique as it is predominantly localized in the endoplasmic reticulum, has constitutive activity and generates H2O2. We hypothesize that these features are consequences of a so far unidentified Nox4-interacting protein. Interacting proteins were screened by quantitative SILAC-Co-immunoprecipitation in HEK293 cells stably overexpressing Nox4. By this technique, several interacting proteins were identified with calnexin showing the most robust interaction.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: SILAC ; LC-MSMS ; macromolecular complexes ; Co-immunoprecipitation
Principal Investigators: (in alphabetical order) |
Ralf Brandes, Institut f�r Kardiovaskul�re Physiologie, Goethe-Universit�t, Frankfurt am Main, Germany, N/A |
Submitting User: | ccms |
Prior KK, Wittig I, Leisegang MS, Groenendyk J, Weissmann N, Michalak M, Jansen-Dürr P, Shah AM, Brandes RP.
The Endoplasmic Reticulum Chaperone Calnexin Is a NADPH Oxidase NOX4 Interacting Protein.
J. Biol. Chem. 2016 Mar 25;291(13):7045-59. Epub 2016 Mar 9.
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